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Article ; Online: Dual transgene amelioration of Lama2-null muscular dystrophy.

McKee, Karen K / Yurchenco, Peter D

Matrix biology : journal of the International Society for Matrix Biology

2023 Volume 118, Page(s) 1–15

Abstract: Null mutations of the Lama2-gene cause a severe congenital muscular dystrophy and associated neuropathy. In the absence of laminin-α2 (Lmα2) there is a compensatory replacement by Lmα4, a subunit that lacks the polymerization and α-dystroglycan (αDG)- ... ...

Abstract	Null mutations of the Lama2-gene cause a severe congenital muscular dystrophy and associated neuropathy. In the absence of laminin-α2 (Lmα2) there is a compensatory replacement by Lmα4, a subunit that lacks the polymerization and α-dystroglycan (αDG)-binding properties of Lmα2. The dystrophic phenotype in the dy
MeSH term(s)	Mice ; Animals ; Muscle, Skeletal/metabolism ; Laminin/genetics ; Laminin/metabolism ; Mice, Transgenic ; Muscular Dystrophies/genetics ; Muscular Dystrophies/metabolism ; Transgenes
Chemical Substances	Laminin
Language	English
Publishing date	2023-03-05
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1183793-7
ISSN	1569-1802 ; 0945-053X
ISSN (online)	1569-1802
ISSN	0945-053X
DOI	10.1016/j.matbio.2023.03.001
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Article ; Online: Amelioration of muscle and nerve pathology of Lama2-related dystrophy by AAV9-laminin-αLN linker protein.

McKee, Karen K / Yurchenco, Peter D

JCI insight

2022 Volume 7, Issue 13

Abstract: LAMA2 deficiency, resulting from a defective or absent laminin α2 subunit, is a common cause of congenital muscular dystrophy. It is characterized by muscle weakness from myofiber degeneration and neuropathy from Schwann cell amyelination. Previously it ... ...

Abstract	LAMA2 deficiency, resulting from a defective or absent laminin α2 subunit, is a common cause of congenital muscular dystrophy. It is characterized by muscle weakness from myofiber degeneration and neuropathy from Schwann cell amyelination. Previously it was shown that transgenic muscle-specific expression of αLNNd, a laminin γ1-binding linker protein that enables polymerization in defective laminins, selectively ameliorates the muscle abnormality in mouse disease models. Here, adeno-associated virus was used to deliver linker mini-genes to dystrophic dy2J/dy2J mice for expression of αLNNd in muscle, or αLNNdΔG2', a shortened linker, in muscle, nerve, and other tissues. Linker and laminin α2 levels were higher in αLNNdΔG2'-treated mice. Both αLNNd- and αLNNdΔG2'-treated mice exhibited increased forelimb grip strength. Further, αLNNdΔG2'-treated mice achieved hind limb and all-limb grip strength levels approaching those of WT mice as well as ablation of hind limb paresis and contractures. This was accompanied by restoration of sciatic nerve axonal envelopment and myelination. Improvement of muscle histology was evident in the muscle-specific αLNNd-expressing mice but more extensive in the αLNNdΔG2'-expressing mice. The results reveal that an αLN linker mini-gene, driven by a ubiquitous promoter, is superior to muscle-specific delivery because of its higher expression that extends to the peripheral nerve. These studies support a potentially novel approach of somatic gene therapy.
MeSH term(s)	Animals ; Laminin/genetics ; Laminin/metabolism ; Mice ; Muscle, Skeletal/metabolism ; Muscular Dystrophies/genetics ; Muscular Dystrophy, Animal/genetics ; Muscular Dystrophy, Animal/metabolism ; Muscular Dystrophy, Animal/pathology ; Peripheral Nerves/metabolism
Chemical Substances	Laminin
Language	English
Publishing date	2022-07-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2379-3708
ISSN (online)	2379-3708
DOI	10.1172/jci.insight.158397
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Article ; Online: Exogenous laminin exhibits a unique vascular pattern in the brain via binding to dystroglycan and integrins.

Ruan, Jingsong / McKee, Karen K / Yurchenco, Peter D / Yao, Yao

Fluids and barriers of the CNS

2022 Volume 19, Issue 1, Page(s) 97

Abstract: Background: Unlike other proteins that exhibit a diffusion pattern after intracerebral injection, laminin displays a vascular pattern. It remains unclear if this unique vascular pattern is caused by laminin-receptor interaction or laminin self-assembly.! ...

Abstract	Background: Unlike other proteins that exhibit a diffusion pattern after intracerebral injection, laminin displays a vascular pattern. It remains unclear if this unique vascular pattern is caused by laminin-receptor interaction or laminin self-assembly. Methods: We compared the distribution of various wild-type laminin isoforms in the brain after intracerebral injection. To determine what causes the unique vascular pattern of laminin in the brain, laminin mutants with impaired receptor-binding and/or self-assembly activities and function-blocking antibodies to laminin receptors were used. In addition, the dynamics of laminin distribution and elimination were examined at multiple time points after intracerebral injection. Results: We found that β2-containing laminins had higher affinity for the vessels compared to β1-containing laminins. In addition, laminin mutants lacking receptor-binding domains but not that lacking self-assembly capability showed substantially reduced vascular pattern. Consistent with this finding, dystroglycan (DAG1) function-blocking antibody significantly reduced the vascular pattern of wild-type laminin-111. Although failed to affect the vascular pattern when used alone, integrin-β1 function-blocking antibody further decreased the vascular pattern when combined with DAG1 antibody. EDTA, which impaired laminini-DAG1 interaction by chelating Ca Conclusions: These findings suggest that intracerebrally injected laminins are enriched in the perivascular space in a receptor (DAG1/integrin)-dependent rather than self-assembly-dependent manner and eliminated from the brain mainly via the perivascular clearance system.
MeSH term(s)	Dystroglycans ; Laminin ; Integrins ; Brain ; Veins
Chemical Substances	Dystroglycans (146888-27-9) ; Laminin ; Integrins
Language	English
Publishing date	2022-12-03
Publishing country	England
Document type	Journal Article
ZDB-ID	2595406-4
ISSN	2045-8118 ; 2045-8118
ISSN (online)	2045-8118
ISSN	2045-8118
DOI	10.1186/s12987-022-00396-y
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Article: Integrating Activities of Laminins that Drive Basement Membrane Assembly and Function.

Yurchenco, Peter D

Current topics in membranes

2015 Volume 76, Page(s) 1–30

Abstract: Studies on extracellular matrix proteins, cells, and genetically modified animals have converged to reveal mechanisms of basement membrane self-assembly as mediated by γ1 subunit-containing laminins, the focus of this chapter. The basic model is as ... ...

Abstract	Studies on extracellular matrix proteins, cells, and genetically modified animals have converged to reveal mechanisms of basement membrane self-assembly as mediated by γ1 subunit-containing laminins, the focus of this chapter. The basic model is as follows: A member of the laminin family adheres to a competent cell surface and typically polymerizes followed by laminin binding to the extracellular adaptor proteins nidogen, perlecan, and agrin. Assembly is completed by the linking of nidogen and heparan sulfates to type IV collagen, allowing it to form a second stabilizing network polymer. The assembled matrix provides structural support, anchoring the extracellular matrix to the cytoskeleton, and acts as a signaling platform. Heterogeneity of function is created in part by the isoforms of laminin that vary in their ability to polymerize and to interact with integrins, dystroglycan, and other receptors. Mutations in laminin subunits, affecting expression or LN domain-specific functions, are a cause of human diseases that include those of muscle, nerve, brain, and kidney.
MeSH term(s)	Animals ; Basement Membrane/metabolism ; Cell Adhesion ; Collagen Type IV/metabolism ; Cytoskeleton/metabolism ; Humans ; Laminin/chemistry ; Laminin/deficiency ; Laminin/metabolism ; Protein Multimerization
Chemical Substances	Collagen Type IV ; Laminin
Language	English
Publishing date	2015
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ISSN	1063-5823
ISSN	1063-5823
DOI	10.1016/bs.ctm.2015.05.001
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Article ; Online: Amelioration of muscle and nerve pathology of Lama2-related dystrophy by AAV9-laminin-αLN linker protein

Karen K. McKee / Peter D. Yurchenco

JCI Insight, Vol 7, Iss

2022 Volume 13

Abstract	LAMA2 deficiency, resulting from a defective or absent laminin α2 subunit, is a common cause of congenital muscular dystrophy. It is characterized by muscle weakness from myofiber degeneration and neuropathy from Schwann cell amyelination. Previously it was shown that transgenic muscle-specific expression of αLNNd, a laminin γ1–binding linker protein that enables polymerization in defective laminins, selectively ameliorates the muscle abnormality in mouse disease models. Here, adeno-associated virus was used to deliver linker mini-genes to dystrophic dy2J/dy2J mice for expression of αLNNd in muscle, or αLNNdΔG2′, a shortened linker, in muscle, nerve, and other tissues. Linker and laminin α2 levels were higher in αLNNdΔG2′-treated mice. Both αLNNd- and αLNNdΔG2′-treated mice exhibited increased forelimb grip strength. Further, αLNNdΔG2′-treated mice achieved hind limb and all-limb grip strength levels approaching those of WT mice as well as ablation of hind limb paresis and contractures. This was accompanied by restoration of sciatic nerve axonal envelopment and myelination. Improvement of muscle histology was evident in the muscle-specific αLNNd-expressing mice but more extensive in the αLNNdΔG2′-expressing mice. The results reveal that an αLN linker mini-gene, driven by a ubiquitous promoter, is superior to muscle-specific delivery because of its higher expression that extends to the peripheral nerve. These studies support a potentially novel approach of somatic gene therapy.
Keywords	Muscle biology ; Neuroscience ; Medicine ; R
Language	English
Publishing date	2022-07-01T00:00:00Z
Publisher	American Society for Clinical investigation
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Organization of the laminin polymer node.

McKee, Karen K / Hohenester, Erhard / Aleksandrova, Maya / Yurchenco, Peter D

Matrix biology : journal of the International Society for Matrix Biology

2021 Volume 98, Page(s) 49–63

Abstract: Laminin polymerization is a key step of basement membrane assembly that depends on the binding of α, β and γ N-terminal LN domains to form a polymer node. Nodal assembly can be divided into two steps consisting of β- and γ-LN dimerization followed by ... ...

Abstract	Laminin polymerization is a key step of basement membrane assembly that depends on the binding of α, β and γ N-terminal LN domains to form a polymer node. Nodal assembly can be divided into two steps consisting of β- and γ-LN dimerization followed by calcium-dependent addition of the α-LN domain. The assembly and structural organization of laminin-111 LN-LEa segments was examined by size-exclusion chromatography (SEC) and electron microscopy. Triskelion-like structures were observed in negatively-stained images of purified α1/β1/γ1 LN-LEa trimers. Image averaging of these revealed a heel-to-toe organization of the LN domains with angled outward projections of the LEa stem-like domains. A series of single-amino acid substitutions was introduced into the polymerization faces of the α1, β1 and γ1 LN domains followed by SEC analysis to distinguish between loss of β-γ mediated dimerization and loss of α-dependent trimerization (with intact β-γ dimers). Dimer-blocking mutations were confined to the γ1-toe and the β1-heel, whereas the trimer-only-blocking mutations mapped to the γ1-heel, β1-toe and the α1-toe and heel. Thus, in the polymer node the γ1-toe pairs with the β1-heel, the β1-toe pairs with the α1-heel, and the α1-toe pairs with the γ1-heel.
MeSH term(s)	Laminin/genetics ; Morphogenesis ; Mutation ; Polymers
Chemical Substances	Laminin ; Polymers
Language	English
Publishing date	2021-05-21
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1183793-7
ISSN	1569-1802 ; 0945-053X
ISSN (online)	1569-1802
ISSN	0945-053X
DOI	10.1016/j.matbio.2021.05.004
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Book: Extracellular matrix assembly and structure

Yurchenco, Peter D.

(Biology of extracellular matrix series)

1994

Author's details	ed. by Peter D. Yurchenco
Series title	Biology of extracellular matrix series
Keywords	Extracellular Matrix ; Extracellular Matrix Proteins ; Grundsubstanz ; Proteine
Subject	Matrix ; Keimschicht ; Mutterschicht ; Amorphe Zwischenzellschicht ; Eiweiss ; Protein
Language	English
Size	XI, 468 S. : Ill., graph. Darst
Publisher	Acad. Press
Publishing place	San Diego u.a.
Publishing country	United States
Document type	Book
HBZ-ID	HT006436965
ISBN	0-12-775170-X ; 978-0-12-775170-2
Database	Catalogue ZB MED Medicine, Health

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Shelf mark	Loan status	Location
1994 A 4947	order for loan	Magazin

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Article ; Online: Cryo-EM reveals the molecular basis oflaminin polymerization and LN-lamininopathies.

Kulczyk, Arkadiusz W / McKee, Karen K / Zhang, Ximo / Bizukojc, Iwona / Yu, Ying Q / Yurchenco, Peter D

Nature communications

2023 Volume 14, Issue 1, Page(s) 317

Abstract: Laminin polymerization is the major step in basement membranes assembly. Its failures cause laminin N-terminal domain lamininopathies including Pierson syndrome. We have employed cryo-electron microscopy to determine a 3.7 Å structure of the trimeric ... ...

Abstract	Laminin polymerization is the major step in basement membranes assembly. Its failures cause laminin N-terminal domain lamininopathies including Pierson syndrome. We have employed cryo-electron microscopy to determine a 3.7 Å structure of the trimeric laminin polymer node containing α1, β1 and γ1 subunits. The structure reveals the molecular basis of calcium-dependent formation of laminin lattice, and provides insights into polymerization defects manifesting in human disease.
MeSH term(s)	Humans ; Laminin/chemistry ; Cryoelectron Microscopy ; Polymerization ; Nephrotic Syndrome ; Pupil Disorders ; Basement Membrane/chemistry
Chemical Substances	Laminin
Language	English
Publishing date	2023-01-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-36077-z
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Article: Linker Protein Repair of LAMA2 Dystrophic Neuromuscular Basement Membranes.

Yurchenco, Peter D / McKee, Karen K

Frontiers in molecular neuroscience

2019 Volume 12, Page(s) 305

Abstract: An understanding of basement membrane (BM) assembly at a molecular level provides a foundation with which to develop repair strategies for diseases with defects of BM structure. As currently understood, laminins become anchored to cell surfaces through ... ...

Abstract	An understanding of basement membrane (BM) assembly at a molecular level provides a foundation with which to develop repair strategies for diseases with defects of BM structure. As currently understood, laminins become anchored to cell surfaces through receptor-mediated interactions and polymerize. This provisional matrix binds to proteoglycans, nidogens and type IV collagen to form a mature BM. Identification of BM binding domains and their binding targets has enabled investigators to engineer proteins that link BM components to modify and improve their functions. This approach is illustrated by the development of two linker proteins to repair the LAMA2-deficient muscular dystrophy (LAMA2-MD). Dystrophy-causing mutations of the
Language	English
Publishing date	2019-12-13
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2452967-9
ISSN	1662-5099
ISSN	1662-5099
DOI	10.3389/fnmol.2019.00305
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Article ; Online: Basement membranes: cell scaffoldings and signaling platforms.

Yurchenco, Peter D

Cold Spring Harbor perspectives in biology

2011 Volume 3, Issue 2

Abstract: Basement membranes are widely distributed extracellular matrices that coat the basal aspect of epithelial and endothelial cells and surround muscle, fat, and Schwann cells. These extracellular matrices, first expressed in early embryogenesis, are self- ... ...

Abstract	Basement membranes are widely distributed extracellular matrices that coat the basal aspect of epithelial and endothelial cells and surround muscle, fat, and Schwann cells. These extracellular matrices, first expressed in early embryogenesis, are self-assembled on competent cell surfaces through binding interactions among laminins, type IV collagens, nidogens, and proteoglycans. They form stabilizing extensions of the plasma membrane that provide cell adhesion and that act as solid-phase agonists. Basement membranes play a role in tissue and organ morphogenesis and help maintain function in the adult. Mutations adversely affecting expression of the different structural components are associated with developmental arrest at different stages as well as postnatal diseases of muscle, nerve, brain, eye, skin, vasculature, and kidney.
MeSH term(s)	Animals ; Axons/physiology ; Basement Membrane/metabolism ; Basement Membrane/physiology ; Cell Adhesion/physiology ; Cell Movement/physiology ; Collagen Type IV/metabolism ; Dystroglycans/metabolism ; Humans ; Integrins/metabolism ; Kidney Glomerulus/physiology ; Laminin/metabolism ; Morphogenesis/physiology ; Receptors, Cell Surface/metabolism ; Signal Transduction/physiology
Chemical Substances	Collagen Type IV ; Integrins ; Laminin ; Receptors, Cell Surface ; Dystroglycans (146888-27-9)
Language	English
Publishing date	2011-02-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ISSN	1943-0264
ISSN (online)	1943-0264
DOI	10.1101/cshperspect.a004911
Database	MEDical Literature Analysis and Retrieval System OnLINE

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