Cathepsin protein

Sulphatides, glycolipids, glycosaminoglycans Galactosialidosis (protective protein/cathepsin A) protective protein/cathepsin A 20... 

Pederson ED, Stanke SR, Whitener SJ, Sebastiani PT, Lamberts BL, Turner DW. Salivary levels of a2-macroglobulin, ai-antitrypsin, c-reactive protein, cathepsin G and elastase in humans with or without destructive periodontal disease. Archs. Oral. Biol. 1995 40 1151-1155. 

Galactosialidosis Protective protein/ cathepsin A Sialyl-OS GM2, GM3, GMl, GDla... 

See also Protein Turnover, Programmed Destruction of Proteins, Cathepsins, Proteasome... 

D. Wang, S. Zaitsev, G. Taylor, A. d Azzo, and E. Bonten, Protective protein/ cathepsin A rescues N-glycosylation defects in neuraminidase-1, Biochim. Biophys. Acta, 1790 (2009) 275-282. 

A. van der Spoel, E. Bonten, and A. d Azzo, Transport of human lysosomal neuraminidase to mature lysosomes requires proteetive protein/cathepsin A, EMBOJ, 17 (1998) 1588-1597. 

E. J. Bonten and A. d Azzo, Lysosomal neuraminidase. Catalytic activation in insect cells is eontrolled by the protective protein/cathepsin A, J. Biol. Chem., 275 (2000) 37657-37663. 

Two general considerations argue against transpeptidation as an important mechanism by which peptide chains are lengthened, whether by amide replacement or by replacement from y-glutamyl or glycyl peptides. The first is the matter of specific amino acid pattern in peptides and proteins. Cathepsin, like chymotrypsin, is acceptor specific, and the... 

Cathepsin D Spleen, liver, and many other animal tissues Lysosomal digestion of proteins... 

Cathepsins are intracellular proteinases that reside within lysosomes or specific intracellular granules. Cathepsins are used to degrade proteins or pqffides that are internalised from the extracellular space. Some cathepsins such as cathepsin-G or cathepsin-K may be released from the cell to degrade specific extracellular matrix proteins. All cathepsins except cathepsin-G (serine) and cathepsin-D (aspartyl) are cysteine proteinases. 

Besides AT, heparin cofactor II (HCII) is an antic-oagulatory protein enhanced by heparin. HCII inactivates thrombin and the nonclotting enzymes cathepsin-G and chymotrypsin. 

Cleavage occur s at the scissile bond. Residues in the substrate towards the N-terminus are numbered PI, P2, P3, etc, whereas residues towards the C-terminus are numbered PI, P2, P3 etc. Cleavage occurs between PI and P1. For a peptidase with limited specificity, only the residue in PI or PI is important for specificity. A peptidase with an extended substrate binding site will have a preference for residues in other positions. For example cathepsin L prefers substrates with phenylalanine in P2 and arginine in PI. However, this is a preference only, and cathepsin L cleaves substrates after other amino acids. Caspase-3 has a preference for Asp in both P4 and PI, but it is unusual for substrate specificity to extend much further from the scissile bond. The peptidase with the most extended substrate specificity may be mitochondrial intermediate peptidase that removes an octopeptide targeting signal from the N-terminus of cytoplasmically synthesized proteins that are destined for import into the mitochondrial lumen. 

Wolf M, Clark-Lewis I, Buii C et al (2003) Cathepsin D specifically cleaves the chemokines macrophage inflammatory protein-1 alpha, macrophage inflammatory protein-1 beta, and SLC that are expressed in human breast cancer. Am J Pathol 162 1183-1190... 

CAH Chronic active hepatitis CALLA Common lymphoblastic leukaemia antigen CALX Conjunctival associated lymphoid tissue CaM Calmodulin cAMP Cyclic adenosine monophosphate also knomt as adenosine 3, 5 -phosphate CAM CeU adhesion molecule CAP57 Cationic protein from neutrophils CAT Catalase CatG Cathepsin G... 

Shimizu, K., Cha, J., Stucky, G.D. and Morse, D.E. (1998) Silicatein alpha Cathepsin L-like protein in sponge biosilica. Proceedings of the National Academy of Sciences of the United States of America, 95, 6234-6238. 

---