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  1. Article: Variants of human L1 cell adhesion molecule arise through alternate splicing of RNA.

    Reid, R A / Hemperly, J J

    Journal of molecular neuroscience : MN

    1992  Volume 3, Issue 3, Page(s) 127–135

    Abstract: The L1 cell adhesion molecule was initially identified and characterized in mouse as a cell-surface glycoprotein that mediates neuron-neuron and neuron-Schwann cell adhesion. We have characterized L1 in humans using cDNA structural and mRNA expression ... ...

    Abstract The L1 cell adhesion molecule was initially identified and characterized in mouse as a cell-surface glycoprotein that mediates neuron-neuron and neuron-Schwann cell adhesion. We have characterized L1 in humans using cDNA structural and mRNA expression analyses. We present the entire coding sequence for human L1, which predicts a 1253-amino acid protein displaying a signal sequence, transmembrane segment, RGD sequence, and potential glycosylation and phosphorylation sites. Nucleotide and deduced amino acid sequence identities between human and mouse L1 are 85% and 87%, respectively. In contrast, the amino acid identity between human L1 and the L1-related molecule chicken Ng-CAM is only 45%. Using Northern blot analyses, a single L1 transcript of 5.5 kb is detected in human fetal brain and in neuroblastoma (IMR-32) and retinoblastoma (Y-79) cell lines. L1 is also expressed in the rhabdomyosarcoma cell lines RD and A-204, which display several muscle characteristics. Two forms of L1, which differ by the presence or absence of a 12-bp cytoplasmic segment, are expressed in both human and mouse. This segment is encoded by a single exon that can be alternately spliced to give rise to the two forms, which appear to be expressed in tissue-specific patterns.
    MeSH term(s) Amino Acid Sequence ; Animals ; Base Sequence ; Cell Adhesion ; Cell Adhesion Molecules, Neuronal/biosynthesis ; Cell Adhesion Molecules, Neuronal/genetics ; DNA/genetics ; Gene Expression ; Genes ; Genetic Variation ; Humans ; Leukocyte L1 Antigen Complex ; Mice/genetics ; Molecular Sequence Data ; Polymerase Chain Reaction ; RNA Splicing ; RNA, Messenger/metabolism ; Sequence Homology, Nucleic Acid
    Chemical Substances Cell Adhesion Molecules, Neuronal ; Leukocyte L1 Antigen Complex ; RNA, Messenger ; DNA (9007-49-2)
    Language English
    Publishing date 1992
    Publishing country United States
    Document type Comparative Study ; Journal Article
    ZDB-ID 1043392-2
    ISSN 0895-8696
    ISSN 0895-8696
    DOI 10.1007/bf02919404
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    Zs.A 3006: Show issues Location:
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  2. Article: Favin versus concanavalin A: Circularly permuted amino acid sequences.

    Cunningham, B A / Hemperly, J J / Hopp, T P / Edelman, G M

    Proceedings of the National Academy of Sciences of the United States of America

    2002  Volume 76, Issue 7, Page(s) 3218–3222

    Abstract: We have determined the tentative amino acid sequence of the beta chain (M(r) 20,000) of the lectin favin. In previous studies, we have shown that the alpha chain (M(r) 5600) of this lectin is homologous to a region in the middle of the concanavalin A ( ... ...

    Abstract We have determined the tentative amino acid sequence of the beta chain (M(r) 20,000) of the lectin favin. In previous studies, we have shown that the alpha chain (M(r) 5600) of this lectin is homologous to a region in the middle of the concanavalin A (Con A) sequence (residues 70-119). Now we present evidence that the beta chain is homologous to two discrete segments of Con A. The homology begins at residue 120 of Con A, extends to the COOH terminus (residue 237) and continues without interruption through the NH(2)-terminal 69 residues of Con A. Together, the alpha and beta chains of favin account for a polypeptide chain equivalent in size to that of Con A. The comparison of the two proteins thus reveals a circular permutation of extensive homologous sequences. The favin molecule contains residues identical to many of the residues postulated to be involved in sugar binding by Con A, and contains all of the direct metal ligands as well as residues homologous to most of the residues that form the beta-pleated sheets of Con A. These homologies suggest that the three-dimensional structures of the two lectins are likely to be very similar. Moreover, favin appears to be even more closely related in primary structure and sugar specificity to the lectins from pea and lentil, raising the possibility that all of these lectins may have structures that resemble Con A. Some of these similarities may also extend to the lectins from soybean, peanut, and red kidney bean, which have different sugar specificities but share sequence homologies with the favin beta chain.
    Language English
    Publishing date 2002-09-13
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.76.7.3218
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  3. Article: Human N-cadherin: nucleotide and deduced amino acid sequence.

    Reid, R A / Hemperly, J J

    Nucleic acids research

    1990  Volume 18, Issue 19, Page(s) 5896

    MeSH term(s) Amino Acid Sequence ; Animals ; Base Sequence ; Cadherins/genetics ; Humans ; Molecular Sequence Data ; Multigene Family ; Polymerase Chain Reaction ; Sequence Homology, Nucleic Acid
    Chemical Substances Cadherins
    Language English
    Publishing date 1990-10-11
    Publishing country England
    Document type Journal Article
    ZDB-ID 186809-3
    ISSN 0305-1048 ; 0301-5610
    ISSN 0305-1048 ; 0301-5610
    DOI 10.1093/nar/18.19.5896
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    Zs.A 1067: Show issues Location:
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  4. Article: N-cadherin expression and function in cultured oligodendrocytes.

    Payne, H R / Hemperly, J J / Lemmon, V

    Brain research. Developmental brain research

    1996  Volume 97, Issue 1, Page(s) 9–15

    Abstract: N-Cadherin is a major cell adhesion molecule that is expressed in the developing nervous system where it has been implicated in neural migration and axon growth. Recently, a role for N-cadherin in oligodendrocyte differentiation has been identified [23]. ...

    Abstract N-Cadherin is a major cell adhesion molecule that is expressed in the developing nervous system where it has been implicated in neural migration and axon growth. Recently, a role for N-cadherin in oligodendrocyte differentiation has been identified [23]. Oligodendrocyte precursors adhere to N-cadherin and mature rapidly to produce myelin sheets. Since this implies that oligodendrocytes express N-cadherin, we examined the expression of N-cadherin by oligodendrocytes in culture. N-Cadherin was expressed by O-2A progenitors, immature oligodendrocytes and mature oligodendrocytes, but at a lower level than in type 1 astrocytes in the same cultures. On mature oligodendrocytes, the N-cadherin was concentrated on the major processes emerging from the soma. The ability of N-cadherin and merosin to promote oligodendrocyte precursor migration was also studied. Average migration rates were significantly higher on merosin (11.2 microns/h) than on N-cadherin (5.6 microns/h). These results suggest that N-cadherin is not likely to function predominantly as a substrate that stimulates migration of O-2A progenitors, but may be more important in initiating early oligodendrocyte-axon interactions that promote the process of myelination.
    MeSH term(s) Animals ; Cadherins/biosynthesis ; Cadherins/pharmacology ; Cadherins/physiology ; Cell Adhesion/drug effects ; Cell Adhesion/physiology ; Cell Movement/drug effects ; Cell Movement/physiology ; Cells, Cultured/chemistry ; Cells, Cultured/drug effects ; Cells, Cultured/metabolism ; Chick Embryo ; Immunoblotting ; Laminin/pharmacology ; Oligodendroglia/chemistry ; Oligodendroglia/cytology ; Oligodendroglia/metabolism ; Optic Nerve/cytology ; Rats ; Serum Albumin, Bovine/pharmacology ; Stem Cells/chemistry ; Stem Cells/cytology ; Stem Cells/metabolism
    Chemical Substances Cadherins ; Laminin ; Serum Albumin, Bovine (27432CM55Q)
    Language English
    Publishing date 1996-11-22
    Publishing country Netherlands
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 8213-2
    ISSN 1872-6755 ; 0165-3806
    ISSN (online) 1872-6755
    ISSN 0165-3806
    DOI 10.1016/s0165-3806(96)00124-1
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    Zs.A 1615: Show issues Location:
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  5. Article: CSF N-CAM in neuroleptic-naïve first-episode patients with schizophrenia.

    Vawter, M P / Hemperly, J J / Freed, W J / Garver, D L

    Schizophrenia research

    1998  Volume 34, Issue 3, Page(s) 123–131

    Abstract: An increased concentration of neural cell adhesion molecule (N-CAM) 105-115 kDa has been reported in patients with schizophrenia in both CSF and in post-mortem brain samples. To determine whether increased N-CAM is integral to the disease process or, ... ...

    Abstract An increased concentration of neural cell adhesion molecule (N-CAM) 105-115 kDa has been reported in patients with schizophrenia in both CSF and in post-mortem brain samples. To determine whether increased N-CAM is integral to the disease process or, alternatively, results from early treatment, CSF N-CAM was measured in a blind study of first episode (FE) patients, who were either neuroleptic-naïve (NN) or neuroleptic-treated (NT, < 100 mg Haldol equivalents), multi-episode (ME) patients, and controls. Overall, the FE patients displayed lower N-CAM concentrations as compared to controls (p = 0.043). This decrease in N-CAM in FE patients was seen only in the FE-NT group as compared to both controls (p = 0.0006). The FE-NT group also showed a lower CSF N-CAM compared to that in the FE-NN (p = 0.025) group. No difference in CSF N-CAM between the FE-NN and control group was found. ME patients showed an increased N-CAM as compared with FE patients (p = 0.018), but not as compared to controls (p = 0.93). Neuroleptic-naïve first-episode patients do not display a phenotypic increase in N-CAM. Thus, N-CAM is altered in first-episode patients following acute neuroleptic treatment and withdrawal, as compared to neuroleptic-naïve first-episode patients.
    MeSH term(s) Adult ; Antipsychotic Agents/therapeutic use ; Female ; Humans ; Male ; Neural Cell Adhesion Molecules/cerebrospinal fluid ; Schizophrenia/cerebrospinal fluid ; Schizophrenia/drug therapy
    Chemical Substances Antipsychotic Agents ; Neural Cell Adhesion Molecules
    Language English
    Publishing date 1998-11-30
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 639422-x
    ISSN 1573-2509 ; 0920-9964
    ISSN (online) 1573-2509
    ISSN 0920-9964
    DOI 10.1016/s0920-9964(98)00103-0
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    Zs.A 2351: Show issues Location:
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  6. Article: NCAM140 interacts with the focal adhesion kinase p125(fak) and the SRC-related tyrosine kinase p59(fyn).

    Beggs, H E / Baragona, S C / Hemperly, J J / Maness, P F

    The Journal of biological chemistry

    1997  Volume 272, Issue 13, Page(s) 8310–8319

    Abstract: Axonal growth cones respond to adhesion molecules and extracellular matrix components by rapid morphological changes and growth rate modification. Neurite outgrowth mediated by the neural cell adhesion molecule (NCAM) requires the src family tyrosine ... ...

    Abstract Axonal growth cones respond to adhesion molecules and extracellular matrix components by rapid morphological changes and growth rate modification. Neurite outgrowth mediated by the neural cell adhesion molecule (NCAM) requires the src family tyrosine kinase p59(fyn) in nerve growth cones, but the molecular basis for this interaction has not been defined. The NCAM140 isoform, which is found in migrating growth cones, selectively co-immunoprecipitated with p59(fyn) from nonionic detergent (Brij 96) extracts of early postnatal mouse cerebellum and transfected rat B35 neuroblastoma and COS-7 cells. p59(fyn) did not associate significantly with the NCAM180 isoform, which is found at sites of stable neural cell contacts, or with the glycophosphatidylinositol-linked NCAM120 isoform. pp60(c-)src, a tyrosine kinase that promotes neurite growth on the neuronal cell adhesion molecule L1, did not interact with any NCAM isoform. Whereas p59(fyn) was constitutively associated with NCAM140, the focal adhesion kinase p125(fak), a nonreceptor tyrosine kinase known to mediate integrin-dependent signaling, became recruited to the NCAM140-p59(fyn) complex when cells were reacted with antibodies against the extracellular region of NCAM. Treatment of cells with a soluble NCAM fusion protein or with NCAM antibodies caused a rapid and transient increase in tyrosine phosphorylation of p125(fak) and p59(fyn). These results suggest that NCAM140 binding interactions at the cell surface induce the assembly of a molecular complex of NCAM140, p125(fak), and p59(fyn) and activate the catalytic function of these tyrosine kinases, initiating a signaling cascade that may modulate growth cone migration.
    MeSH term(s) Animals ; COS Cells ; Cell Adhesion Molecules/metabolism ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; Mice ; Molecular Weight ; Neural Cell Adhesion Molecules/metabolism ; Phosphoproteins/metabolism ; Protein-Tyrosine Kinases/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-fyn ; Rats ; Receptor, Insulin/metabolism ; Transfection
    Chemical Substances Cell Adhesion Molecules ; Neural Cell Adhesion Molecules ; Phosphoproteins ; Proto-Oncogene Proteins ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; Receptor, Insulin (EC 2.7.10.1) ; Focal Adhesion Kinase 1 (EC 2.7.10.2) ; Focal Adhesion Protein-Tyrosine Kinases (EC 2.7.10.2) ; Fyn protein, mouse (EC 2.7.10.2) ; Fyn protein, rat (EC 2.7.10.2) ; Proto-Oncogene Proteins c-fyn (EC 2.7.10.2) ; Ptk2 protein, mouse (EC 2.7.10.2) ; Ptk2 protein, rat (EC 2.7.10.2)
    Language English
    Publishing date 1997-03-28
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.272.13.8310
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  7. Article: Monoclonal antibody interaction with the third immunoglobulin-like domain of N-CAM is sufficient to cause cell migration.

    Ackley, R L / Madison, R D / Archibald, S J / Hemperly, J J

    Molecular and cellular neurosciences

    1997  Volume 10, Issue 1-2, Page(s) 117–129

    Abstract: Cellular adhesion molecules can influence a variety of biological mechanisms in the nervous system. These range from the processes of normal development and maintenance to neural plasticity and recovery following injury. The elucidation of the intricate ... ...

    Abstract Cellular adhesion molecules can influence a variety of biological mechanisms in the nervous system. These range from the processes of normal development and maintenance to neural plasticity and recovery following injury. The elucidation of the intricate contributions of these molecules will require the correlation of functional assays with specific molecules and the specific binding domains of such molecules with multiple signaling pathways. The data presented in this paper show that the monoclonal antibody anti-NCAM16, directed against the third immunoglobulin-like domain of the neural cell adhesion molecule N-CAM, is capable of stimulating the complex biological process of cell migration in primary embryonic motor neurons and human neuronal cell lines.
    MeSH term(s) Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/pharmacology ; Cell Movement/physiology ; Cells, Cultured ; Humans ; Immunoglobulins/chemistry ; Motor Neurons/drug effects ; Motor Neurons/physiology ; Muscles/chemistry ; Nerve Growth Factors/pharmacology ; Neural Cell Adhesion Molecules/chemistry ; Neural Cell Adhesion Molecules/immunology ; Neural Cell Adhesion Molecules/pharmacology ; Neurons/drug effects ; Neurons/physiology ; Peptide Fragments/chemistry ; Peptide Fragments/genetics ; Peptide Fragments/immunology ; Rats/embryology ; Rats, Sprague-Dawley ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/pharmacology ; Tissue Extracts/pharmacology ; Tumor Cells, Cultured
    Chemical Substances Antibodies, Monoclonal ; Immunoglobulins ; Nerve Growth Factors ; Neural Cell Adhesion Molecules ; Peptide Fragments ; Recombinant Fusion Proteins ; Tissue Extracts
    Language English
    Publishing date 1997
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1046640-x
    ISSN 1095-9327 ; 1044-7431
    ISSN (online) 1095-9327
    ISSN 1044-7431
    DOI 10.1006/mcne.1997.0645
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    Zs.A 3035: Show issues Location:
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  8. Article: Expression of neural cell adhesion molecule in normal and neoplastic human neuroendocrine tissues.

    Jin, L / Hemperly, J J / Lloyd, R V

    The American journal of pathology

    1991  Volume 138, Issue 4, Page(s) 961–969

    Abstract: The neural cell adhesion molecule (N-CAM) is a group of cell surface glycoproteins involved in direct cell--cell adhesion. N-CAM expression in normal and neoplastic tissues was examined with specific antibodies and oligonucleotide probes by ... ...

    Abstract The neural cell adhesion molecule (N-CAM) is a group of cell surface glycoproteins involved in direct cell--cell adhesion. N-CAM expression in normal and neoplastic tissues was examined with specific antibodies and oligonucleotide probes by immunohistochemistry and in situ hybridization. Most neuroendocrine cells and tumors with secretory granules expressed N-CAM protein and mRNA. Parathyroid adenomas (4) were somewhat unusual, because N-CAM mRNA, but not protein, was detected in some of these benign neoplasms. Most non-neuroendocrine cells and tumors did not express N-CAM, although uterine smooth muscle and an adrenal cortical carcinoma were both positive. Western blots disclosed proteins of 180, 140, and 120 kd in normal adult brain, whereas two pheochromocytomas, a null cell adenoma, and a gastrinoma had proteins of approximately 180 and 140 kd. These results indicate that N-CAM protein and mRNA are widely expressed in neuroendocrine cells and neoplasms. N-CAM oligonucleotide probes as well as antibodies against N-CAM can be used as broad-spectrum neuroendocrine markers. In addition, these molecular probes can be used to examine the role of N-CAM in the development and regulation of neuroendocrine tissues.
    MeSH term(s) Cell Adhesion Molecules, Neuronal/metabolism ; Endocrine Glands/metabolism ; Endocrine System Diseases/metabolism ; Humans ; Immunoblotting ; Immunohistochemistry ; Nervous System/metabolism ; Nervous System Neoplasms/metabolism ; Nucleic Acid Hybridization ; Reference Values
    Chemical Substances Cell Adhesion Molecules, Neuronal
    Language English
    Publishing date 1991-04
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2943-9
    ISSN 1525-2191 ; 0002-9440
    ISSN (online) 1525-2191
    ISSN 0002-9440
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  9. Article: Novel fluorescent technology platform for high throughput cytotoxicity and proliferation assays.

    Wodnicka, M / Guarino, R D / Hemperly, J J / Timmins, M R / Stitt, D / Pitner, J B

    Journal of biomolecular screening

    2000  Volume 5, Issue 3, Page(s) 141–152

    Abstract: We have developed a novel fluorescent Oxygen BioSensor technology platform adaptable to many applications in the area of drug discovery and development, particularly cell-based assays. This biosensor technology requires no additional reagents or ... ...

    Abstract We have developed a novel fluorescent Oxygen BioSensor technology platform adaptable to many applications in the area of drug discovery and development, particularly cell-based assays. This biosensor technology requires no additional reagents or incubations, and affords continuous real-time readout of dissolved oxygen concentrations. Since the level of oxygen dissolved in an assay's medium correlates to the number and viability of the cells in the medium, this technology is ideally suited for monitoring cell viability, proliferation, or death. The technology is particularly well suited to investigating cells' kinetic responses to proliferative or toxic stimuli, such as drugs. When incorporated into a 96- or 384-well microplate format, it is compatible with standard laboratory automation systems. Here we present data illustrating the application of the Oxygen BioSensor technology for rapid, homogeneous detection and evaluation of metabolic activity of a variety of eukaryotic and prokaryotic cells, including mammalian cells, insect cells, yeast, and bacteria. In the absence of toxic substances, we find a good correlation between cell number and signal over a wide range of cell concentrations and growth times. To evaluate the usefulness of the Oxygen BioSensor for cytotoxicity assays, we have performed a series of experiments using a range of toxic agents and cell types, including both bacteria and mammalian cell lines. In a side-by-side comparison to standard MTT assays using HL60 cells, comparable IC(50) values were found with the Oxygen BioSensor for five different toxins or drugs. This assay method does not have the need for additional reagents, handling steps, or incubation periods required by the MTT assays.
    MeSH term(s) Animals ; Anti-Bacterial Agents/pharmacology ; Biosensing Techniques ; Cell Division/drug effects ; Cell Line ; Fluorescent Dyes ; Humans ; Microbial Sensitivity Tests ; Oxygen ; Spectrometry, Fluorescence/methods
    Chemical Substances Anti-Bacterial Agents ; Fluorescent Dyes ; Oxygen (S88TT14065)
    Language English
    Publishing date 2000-06
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1433680-7
    ISSN 1552-454X ; 1087-0571
    ISSN (online) 1552-454X
    ISSN 1087-0571
    DOI 10.1177/108705710000500306
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    Zs.A 4911: Show issues Location:
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  10. Article: Identification and characterization of the human cell adhesion molecule contactin.

    Reid, R A / Bronson, D D / Young, K M / Hemperly, J J

    Brain research. Molecular brain research

    1994  Volume 21, Issue 1-2, Page(s) 1–8

    Abstract: We have prepared a monoclonal antibody, Neuro-1, that recognizes the human homolog of the chicken contactin/F11 and mouse F3 cell adhesion molecules. The Neuro-1 antigen, structurally characterized as a 135 kDa glycosylphosphatidylinositol-linked ... ...

    Abstract We have prepared a monoclonal antibody, Neuro-1, that recognizes the human homolog of the chicken contactin/F11 and mouse F3 cell adhesion molecules. The Neuro-1 antigen, structurally characterized as a 135 kDa glycosylphosphatidylinositol-linked glycoprotein, was immunoaffinity purified and partially sequenced. Comparison of an internal peptide sequence to that predicted from the chicken contactin/F11, mouse F3 and human contactin (reported herein) cDNA sequence identifies the Neuro-1 antigen as human contactin. Moreover, a polyclonal antisera generated against the purified Neuro-1 antigen was immunoreactive with a fragment of human contactin expressed in bacteria. The complete coding and deduced amino acid sequences of human contactin were determined and are 86% and 95% identical to the respective mouse F3 sequences. Structural features shared with contactin/F11/F3 include six immunoglobulin type C2 and four fibronectin type III-like domains, multiple sites for asn-linked glycosylation and a COOH-terminal signal peptide presumably removed during the generation of a phosphatidylinositol cell surface linkage. The potential for glycosylation and GPI-linkage is also consistent with protein chemical studies of human contactin. Contactin mRNA expression was characterized using Northern blot analyses of human tissues and cell lines. High level expression of a single contactin transcript in adult brain, and low level expression of multiple transcripts in lung, pancreas, kidney and skeletal muscle are observed. Highly expressed multiple transcripts, similar in pattern to that of pancreas, lung, kidney and skeletal muscle, are also observed in human neuroblastoma and retinoblastoma cell lines.
    MeSH term(s) Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Base Sequence ; Cell Adhesion ; Cell Adhesion Molecules, Neuronal ; Cell Line ; Chickens ; Cloning, Molecular ; Contactins ; DNA Primers ; DNA, Complementary/chemistry ; DNA, Complementary/metabolism ; Gene Library ; Humans ; Mice ; Molecular Sequence Data ; Molecular Weight ; Nerve Tissue Proteins/analysis ; Nerve Tissue Proteins/biosynthesis ; Nerve Tissue Proteins/genetics ; Organ Specificity ; Polymerase Chain Reaction ; RNA, Messenger/biosynthesis ; RNA, Messenger/metabolism ; Recombinant Proteins/analysis ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/isolation & purification ; Sequence Homology, Amino Acid ; Transcription, Genetic
    Chemical Substances Antibodies, Monoclonal ; Cell Adhesion Molecules, Neuronal ; Contactins ; DNA Primers ; DNA, Complementary ; Nerve Tissue Proteins ; RNA, Messenger ; Recombinant Proteins
    Language English
    Publishing date 1994-01
    Publishing country Netherlands
    Document type Comparative Study ; Journal Article
    ZDB-ID 632883-0
    ISSN 1872-6941 ; 0169-328X
    ISSN (online) 1872-6941
    ISSN 0169-328X
    DOI 10.1016/0169-328x(94)90372-7
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