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Article ; Online: Impaired activity and membrane association of most calpain-5 mutants causal for neovascular inflammatory vitreoretinopathy.

Geddes, James W / Bondada, Vimala / Croall, Dorothy E / Rodgers, David W / Gal, Jozsef

Biochimica et biophysica acta. Molecular basis of disease

2023 Volume 1869, Issue 6, Page(s) 166747

Abstract: Neovascular inflammatory vitreoretinopathy (NIV) is a rare eye disease that ultimately leads to complete blindness and is caused by mutations in the gene encoding calpain-5 (CAPN5), with six pathogenic mutations identified. In transfected SH-SY5Y cells, ... ...

Abstract	Neovascular inflammatory vitreoretinopathy (NIV) is a rare eye disease that ultimately leads to complete blindness and is caused by mutations in the gene encoding calpain-5 (CAPN5), with six pathogenic mutations identified. In transfected SH-SY5Y cells, five of the mutations resulted in decreased membrane association, diminished S-acylation, and reduced calcium-induced autoproteolysis of CAPN5. CAPN5 proteolysis of the autoimmune regulator AIRE was impacted by several NIV mutations. R243, L244, K250 and the adjacent V249 are on β-strands in the protease core 2 domain. Conformational changes induced by Ca
MeSH term(s)	Humans ; Calpain/genetics ; Calpain/metabolism ; Neuroblastoma ; Vitreoretinopathy, Proliferative/genetics ; Vitreoretinopathy, Proliferative/pathology ; Mutation
Chemical Substances	Calpain (EC 3.4.22.-) ; Capn5 protein, human (EC 3.4.22.-)
Language	English
Publishing date	2023-05-18
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	60-7
ISSN	1879-260X ; 1879-2596 ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-260X ; 1879-2596 ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbadis.2023.166747
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Article ; Online: S-acylation regulates the membrane association and activity of Calpain-5.

Gal, Jozsef / Bondada, Vimala / Mashburn, Charles B / Rodgers, David W / Croall, Dorothy E / Geddes, James W

Biochimica et biophysica acta. Molecular cell research

2022 Volume 1869, Issue 9, Page(s) 119298

Abstract: Calpain-5 (CAPN5) is a member of the calpain family of calcium-activated neutral thiol proteases. CAPN5 is partly membrane associated, despite its lack of a transmembrane domain. Unlike classical calpains, CAPN5 contains a C-terminal C2 domain. C2 ... ...

Abstract	Calpain-5 (CAPN5) is a member of the calpain family of calcium-activated neutral thiol proteases. CAPN5 is partly membrane associated, despite its lack of a transmembrane domain. Unlike classical calpains, CAPN5 contains a C-terminal C2 domain. C2 domains often have affinity to lipids, mediating membrane association. We recently reported that the C2 domain of CAPN5 was essential for its membrane association and the activation of its autolytic activity. However, despite the removal of the C2 domain by autolysis, the N-terminal fragment of CAPN5 remained membrane associated. S-acylation, also referred to as S-palmitoylation, is a reversible post-translational lipid modification of cysteine residues that promotes membrane association of soluble proteins. In the present study several S-acylated cysteine residues were identified in CAPN5 with the acyl-PEG exchange method. Data reported here demonstrate that CAPN5 is S-acylated on up to three cysteine residues including Cys-4 and Cys-512, and likely Cys-507. The D589N mutation in a potential calcium binding loop within the C2 domain interfered with the S-acylation of CAPN5, likely preventing initial membrane association. Mutating specific cysteine residues of CAPN5 interfered with both its membrane association and the activation of CAPN5 autolysis. Taken together, our results suggest that the S-acylation of CAPN5 is critical for its membrane localization which appears to favor its enzymatic activity.
MeSH term(s)	Acylation ; Calcium/metabolism ; Calpain/genetics ; Calpain/metabolism ; Cysteine/genetics ; Cysteine/metabolism ; Lipoylation
Chemical Substances	Calpain (EC 3.4.22.-) ; Cysteine (K848JZ4886) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2022-05-26
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2022.119298
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Article ; Online: The C2 domain of calpain 5 contributes to enzyme activation and membrane localization.

Bondada, Vimala / Gal, Jozsef / Mashburn, Charles / Rodgers, David W / Larochelle, Katherine E / Croall, Dorothy E / Geddes, James W

Biochimica et biophysica acta. Molecular cell research

2021 Volume 1868, Issue 7, Page(s) 119019

Abstract: The enzymatic characteristics of the ubiquitous calpain 5 (CAPN5) remain undescribed despite its high expression in the central nervous system and links to eye development and disease. CAPN5 contains the typical protease core domains but lacks the C ... ...

Abstract	The enzymatic characteristics of the ubiquitous calpain 5 (CAPN5) remain undescribed despite its high expression in the central nervous system and links to eye development and disease. CAPN5 contains the typical protease core domains but lacks the C terminal penta-EF hand domain of classical calpains, and instead contains a putative C2 domain. This study used the SH-SY5Y neuroblastoma cell line stably transfected with CAPN5-3xFLAG variants to assess the potential roles of the CAPN5 C2 domain in Ca
MeSH term(s)	Amino Acid Sequence/genetics ; C2 Domains/genetics ; C2 Domains/physiology ; Calpain/genetics ; Calpain/metabolism ; Cell Movement ; Enzyme Activation/genetics ; Humans ; Models, Molecular ; Mutation/genetics ; Protein Conformation ; Protein Domains/physiology
Chemical Substances	Calpain (EC 3.4.22.-) ; Capn5 protein, human (EC 3.4.22.-)
Language	English
Publishing date	2021-03-31
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2021.119019
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Article ; Online: The calpains: modular designs and functional diversity.

Croall, Dorothy E / Ersfeld, Klaus

Genome biology

2007 Volume 8, Issue 6, Page(s) 218

Abstract: The calpain family is named for the calcium dependence of the papain-like, thiol protease activity of the well-studied ubiquitous vertebrate enzymes calpain-1 (mu-calpain) and calpain-2 (m-calpain). Proteins showing sequence relatedness to the catalytic ... ...

Abstract	The calpain family is named for the calcium dependence of the papain-like, thiol protease activity of the well-studied ubiquitous vertebrate enzymes calpain-1 (mu-calpain) and calpain-2 (m-calpain). Proteins showing sequence relatedness to the catalytic core domains of these enzymes are included in this ancient and diverse eukaryotic protein family. Calpains are examples of highly modular organization, with several varieties of amino-terminal or carboxy-terminal modules flanking a conserved core. Acquisition of the penta-EF-hand module involved in calcium binding (and the formation of heterodimers for some calpains) seems to be a relatively late event in calpain evolution. Several alternative mechanisms for binding calcium and associating with membranes/phospholipids are found throughout the family. The gene family is expanded in mammals, trypanosomes and ciliates, with up to 26 members in Tetrahymena, for example; in striking contrast to this, only a single calpain gene is present in many other protozoa and in plants. The many isoforms of calpain and their multiple splice variants complicate the discussion and analysis of the family, and challenge researchers to ascertain the relationships between calpain gene sequences, protein isoforms and their distinct or overlapping functions. In mammals and plants it is clear that a calpain plays an essential role in development. There is increasing evidence that ubiquitous calpains participate in a variety of signal transduction pathways and function in important cellular processes of life and death. In contrast to relatively promiscuous degradative proteases, calpains cleave only a restricted set of protein substrates and use complex substrate-recognition mechanisms, involving primary and secondary structural features of target proteins. The detailed physiological significance of both proteolytically active calpains and those lacking key catalytic residues requires further study.
MeSH term(s)	Animals ; Calpain/chemistry ; Calpain/genetics ; Calpain/physiology ; Models, Molecular ; Phylogeny
Chemical Substances	Calpain (EC 3.4.22.-)
Language	English
Publishing date	2007
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
ZDB-ID	2040529-7
ISSN	1474-760X ; 1465-6914 ; 1465-6906
ISSN (online)	1474-760X ; 1465-6914
ISSN	1465-6906
DOI	10.1186/gb-2007-8-6-218
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Article: The calpains: modular designs and functional diversity

Croall, Dorothy E / Klaus Ersfeld

Genome biology. 2007 June, v. 8, no. 6

2007

Abstract: The calpain family is named for the calcium dependence of the papain-like, thiol protease activity of the well-studied ubiquitous vertebrate enzymes calpain-1 (Î¼-calpain) and calpain-2 (m-calpain). Proteins showing sequence relatedness to the catalytic ... ...

Abstract	The calpain family is named for the calcium dependence of the papain-like, thiol protease activity of the well-studied ubiquitous vertebrate enzymes calpain-1 (Î¼-calpain) and calpain-2 (m-calpain). Proteins showing sequence relatedness to the catalytic core domains of these enzymes are included in this ancient and diverse eukaryotic protein family. Calpains are examples of highly modular organization, with several varieties of amino-terminal or carboxy-terminal modules flanking a conserved core. Acquisition of the penta-EF-hand module involved in calcium binding (and the formation of heterodimers for some calpains) seems to be a relatively late event in calpain evolution. Several alternative mechanisms for binding calcium and associating with membranes/phospholipids are found throughout the family. The gene family is expanded in mammals, trypanosomes and ciliates, with up to 26 members in Tetrahymena, for example; in striking contrast to this, only a single calpain gene is present in many other protozoa and in plants. The many isoforms of calpain and their multiple splice variants complicate the discussion and analysis of the family, and challenge researchers to ascertain the relationships between calpain gene sequences, protein isoforms and their distinct or overlapping functions. In mammals and plants it is clear that a calpain plays an essential role in development. There is increasing evidence that ubiquitous calpains participate in a variety of signal transduction pathways and function in important cellular processes of life and death. In contrast to relatively promiscuous degradative proteases, calpains cleave only a restricted set of protein substrates and use complex substrate-recognition mechanisms, involving primary and secondary structural features of target proteins. The detailed physiological significance of both proteolytically active calpains and those lacking key catalytic residues requires further study.
Keywords	calcium ; calpain ; death ; enzyme activity ; evolution ; functional diversity ; genes ; mammals ; nucleotide sequences ; phospholipids ; protein isoforms ; proteins ; Protozoa ; signal transduction ; Tetrahymena ; thiols
Language	English
Dates of publication	2007-06
Size	p. 1438.
Publishing place	Springer-Verlag
Document type	Article
ZDB-ID	2040529-7
ISSN	1474-760X ; 1465-6914 ; 1465-6906
ISSN (online)	1474-760X ; 1465-6914
ISSN	1465-6906
DOI	10.1186/gb-2007-8-6-218
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Article: Detecting the active conformation of calpain with calpastatin-based reagents.

Croall, Dorothy E / Vanhooser, Lisa M / Cashon, Robert E

Biochimica et biophysica acta

2008 Volume 1784, Issue 11, Page(s) 1676–1686

Abstract: The specific, calcium-dependent, high affinity interaction between calpain and its endogenous inhibitor calpastatin was exploited to selectively detect the calcium-bound, catalytically competent, conformation of calpain in vitro. Modification of ... ...

Abstract	The specific, calcium-dependent, high affinity interaction between calpain and its endogenous inhibitor calpastatin was exploited to selectively detect the calcium-bound, catalytically competent, conformation of calpain in vitro. Modification of calpastatin domain-1 (Val(114)-Ser(270)) or its N-terminal fragment (Val(114)-Pro(202)), at selected unique cysteine residues with maleimide-AlexaFluor546 did not compromise calpastatin function (inhibition of calpain) or its binding with calpain. Ca(2+)-dependent binding between catalytically dead calpain-2 (Cys(105)Ala) fused with eGFP and these fluorigenic calpastatin peptides generates fluorescent resonance energy transfer (FRET). The FRET signal documents proximity of calpain-2, C-terminally linked fluorophore to specific sites within calpastatin when the proteins form a complex. These results provide important insights into the calcium-dependent interaction between calpain and calpastatin and for holo-calpain-2 in solution experimentally validate some key features of their predicted interactions. These data also provide proof of concept that the calpastatin-based reagents may be useful to selectively detect the active conformation of calpain.
MeSH term(s)	Amino Acid Sequence ; Calcium/metabolism ; Calcium/pharmacology ; Calcium-Binding Proteins/chemistry ; Calcium-Binding Proteins/metabolism ; Calcium-Binding Proteins/pharmacology ; Calpain/antagonists & inhibitors ; Calpain/chemistry ; Calpain/metabolism ; Catalytic Domain/drug effects ; Cysteine Proteinase Inhibitors/chemistry ; Cysteine Proteinase Inhibitors/pharmacology ; Enzyme Activation/drug effects ; Humans ; Models, Biological ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation/drug effects ; Protein Structure, Tertiary ; Substrate Specificity
Chemical Substances	Calcium-Binding Proteins ; Cysteine Proteinase Inhibitors ; calpastatin (79079-11-1) ; Calpain (EC 3.4.22.-) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2008-08-28
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbapap.2008.08.013
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Article: Casein zymography of calpains using a 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid-imidazole buffer.

Croall, Dorothy E / Moffett, Katherin / Hatch, Harold

Analytical biochemistry

2002 Volume 304, Issue 1, Page(s) 129–132

MeSH term(s)	Animals ; Buffers ; Calpain/isolation & purification ; Caseins ; Cattle ; Electrophoresis, Polyacrylamide Gel/methods ; HEPES ; Imidazoles ; Isoelectric Point ; Isoenzymes/isolation & purification ; Mice ; Rats ; Recombinant Proteins/isolation & purification
Chemical Substances	Buffers ; Caseins ; Imidazoles ; Isoenzymes ; Recombinant Proteins ; Calpain (EC 3.4.22.-) ; HEPES (RWW266YE9I)
Language	English
Publishing date	2002-05-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1110-1
ISSN	1096-0309 ; 0003-2697
ISSN (online)	1096-0309
ISSN	0003-2697
DOI	10.1006/abio.2001.5606
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Article ; Online: m-Calpain is required for preimplantation embryonic development in mice.

Dutt, Previn / Croall, Dorothy E / Arthur, J Simon C / Veyra, Teresa De / Williams, Karen / Elce, John S / Greer, Peter A

BMC developmental biology

2006 Volume 6, Page(s) 3

Abstract: Background: Mu-calpain and m-calpain are ubiquitously expressed proteases implicated in cellular migration, cell cycle progression, degenerative processes and cell death. These heterodimeric enzymes are composed of distinct catalytic subunits, encoded ... ...

Abstract	Background: Mu-calpain and m-calpain are ubiquitously expressed proteases implicated in cellular migration, cell cycle progression, degenerative processes and cell death. These heterodimeric enzymes are composed of distinct catalytic subunits, encoded by Capn1 (mu-calpain) or Capn2 (m-calpain), and a common regulatory subunit encoded by Capn4. Disruption of the mouse Capn4 gene abolished both mu-calpain and m-calpain activity, and resulted in embryonic lethality, thereby suggesting essential roles for one or both of these enzymes during mammalian embryogenesis. Disruption of the Capn1 gene produced viable, fertile mice implying that either m-calpain could compensate for the loss of mu-calpain, or that the loss of m-calpain was responsible for death of Capn4-/- mice. Results: To distinguish between the alternatives described above, we deleted an essential coding region in the mouse Capn2 gene in embryonic stems cells and transmitted this mutant allele through the mouse germline. Breeding of heterozygous animals failed to produce homozygous mutant live offspring or implanted embryos. A nested PCR genotyping protocol was established, and homozygous preimplantation mutant embryos were detected at the morula but not at the blastocyts stage. Conclusion: We conclude that homozygous disruption of the Capn2 gene results in pre-implantation embryonic lethality between the morula and blastocyst stage. This establishes that mu-calpain and m-calpain have distinct functions, and that m-calpain is vital for development of the preimplantation murine embryo.
MeSH term(s)	Animals ; Blastocyst/physiology ; Calpain/genetics ; Chimera/genetics ; Cloning, Molecular ; DNA Primers ; Embryonic Stem Cells/physiology ; Female ; Gene Expression Regulation, Developmental ; Genetic Vectors ; Genotype ; Germ-Line Mutation ; Male ; Mice ; Pregnancy ; Sequence Analysis, DNA
Chemical Substances	DNA Primers ; Calpain (EC 3.4.22.-) ; Capn1 protein, mouse (EC 3.4.22.52)
Language	English
Publishing date	2006-01-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	1471-213X
ISSN (online)	1471-213X
DOI	10.1186/1471-213X-6-3
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Article ; Online: m-Calpain is required for preimplantation embryonic development in mice

Williams Karen / Veyra Teresa De / Arthur J Simon C / Croall Dorothy E / Dutt Previn / Elce John S / Greer Peter A

BMC Developmental Biology, Vol 6, Iss 1, p

2006 Volume 3

Abstract: Abstract Background μ-calpain and m-calpain are ubiquitously expressed proteases implicated in cellular migration, cell cycle progression, degenerative processes and cell death. These heterodimeric enzymes are composed of distinct catalytic subunits, ... ...

Abstract	Abstract Background μ-calpain and m-calpain are ubiquitously expressed proteases implicated in cellular migration, cell cycle progression, degenerative processes and cell death. These heterodimeric enzymes are composed of distinct catalytic subunits, encoded by Capn1 (μ-calpain) or Capn2 (m-calpain), and a common regulatory subunit encoded by Capn4 . Disruption of the mouse Capn4 gene abolished both μ-calpain and m-calpain activity, and resulted in embryonic lethality, thereby suggesting essential roles for one or both of these enzymes during mammalian embryogenesis. Disruption of the Capn1 gene produced viable, fertile mice implying that either m-calpain could compensate for the loss of μ-calpain, or that the loss of m-calpain was responsible for death of Capn4 -/- mice. Results To distinguish between the alternatives described above, we deleted an essential coding region in the mouse Capn 2 gene in embryonic stems cells and transmitted this mutant allele through the mouse germline. Breeding of heterozygous animals failed to produce homozygous mutant live offspring or implanted embryos. A nested PCR genotyping protocol was established, and homozygous preimplantation mutant embryos were detected at the morula but not at the blastocyts stage. Conclusion We conclude that homozygous disruption of the Capn2 gene results in pre-implantation embryonic lethality between the morula and blastocyst stage. This establishes that μ-calpain and m-calpain have distinct functions, and that m-calpain is vital for development of the preimplantation murine embryo.
Keywords	Biology (General) ; QH301-705.5
Subject code	572
Language	English
Publishing date	2006-01-01T00:00:00Z
Publisher	BMC
Document type	Article ; Online
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