» Articles » PMID: 6150482

Lens Transglutaminase Selects Specific Beta-crystallin Sequences As Substrate

Overview
Specialty Science
Date 1984 Nov 1
PMID 6150482
Citations 4
Authors
Affiliations
Soon will be listed here.
Abstract

A Ca2+-dependent transglutaminase (EC 2.3.2.13) has been demonstrated in the eye lenses of several mammalian species [Lorand, L., Hsu, L. K. M., Siefring, G. E., Jr., & Rafferty, N. S. (1981) Proc. Natl. Acad. Sci. USA 78, 1356-1360]. Using [3H]methylamine as a convenient probe for transglutaminase activity, we have explored the action of this enzyme in the bovine eye lens. We could characterize the glutamine residues acting as acyl-donor sites in three beta-crystallin chains, which are the only substrates for lens transglutaminase among the various lens-specific structural proteins, the crystallins. A single glutamine was found to bind [3H]methylamine in each of these three chains: glutamine -9 in beta Bp (beta B2), glutamine -21 in beta B3, and glutamine -23 or -24 in beta A3. The four glutamines are all located in the NH2-terminal regions, which presumably extend from the compact two-domain structure of the beta-crystallin chains. It was, moreover, established that several components of the lens cytoskeleton are substrates for transglutaminase.

Citing Articles

Biological functionalities of transglutaminase 2 and the possibility of its compensation by other members of the transglutaminase family.

Odii B, Coussons P ScientificWorldJournal. 2014; 2014:714561.

PMID: 24778599 PMC: 3981525. DOI: 10.1155/2014/714561.


Stabilization of collagen-tailed acetylcholinesterase in muscle cells through extracellular anchorage by transglutaminase-catalyzed cross-linking.

Hand D, Dias D, Haynes L Mol Cell Biochem. 2000; 204(1-2):65-76.

PMID: 10718626 DOI: 10.1023/a:1007068017315.


Localization of transglutaminase-reactive glutamine residues in bovine osteopontin.

Sorensen E, Rasmussen L, Moller L, Jensen P, Hojrup P, Petersen T Biochem J. 1994; 304 ( Pt 1):13-6.

PMID: 7998923 PMC: 1137443. DOI: 10.1042/bj3040013.


Exposure of beta H-crystallin to hydroxyl radicals enhances the transglutaminase-susceptibility of its existing amine-donor and amine-acceptor sites.

Groenen P, Seccia M, Smulders R, GRAVELA E, Cheeseman K, Bloemendal H Biochem J. 1993; 295 ( Pt 2):399-404.

PMID: 7902086 PMC: 1134895. DOI: 10.1042/bj2950399.

References
1.
UDENFRIEND S, Stein S, Bohlen P, Dairman W, Leimgruber W, Weigele M . Fluorescamine: a reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range. Science. 1972; 178(4063):871-2. DOI: 10.1126/science.178.4063.871. View

2.
van der Ouderaa F, de Jong W, Bloemendal H . The amino-acid sequence of the alphaA2 chain of bovine alpha-crystallin. Eur J Biochem. 1973; 39(1):207-22. DOI: 10.1111/j.1432-1033.1973.tb03119.x. View

3.
Ofarrell P . High resolution two-dimensional electrophoresis of proteins. J Biol Chem. 1975; 250(10):4007-21. PMC: 2874754. View

4.
Rice R, Green H . The cornified envelope of terminally differentiated human epidermal keratinocytes consists of cross-linked protein. Cell. 1977; 11(2):417-22. DOI: 10.1016/0092-8674(77)90059-9. View

5.
Tschesche H . Carboxypeptidase C. Methods Enzymol. 1977; 47:73-84. DOI: 10.1016/0076-6879(77)47009-5. View