Diverse biological functions of extracellular collagen processing enzymes

被引:103
作者
Trackman, PC [1 ]
机构
[1] Boston Univ, Sch Med, Goldman Sch Grad Dent, Divoral Biol,Dept Biochem, Boston, MA 02118 USA
关键词
collagen; extracellular matrix deposition; posttranslational modification; tumor suppressors;
D O I
10.1002/jcb.20605
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Collagens are abundant proteins in higher organ isms, and are formed by a complex biosynthetic pathway involving intracellular and extracellular post-translational modifications. Starting from simple soluble precursors, this interesting pathway produces insoluble functional fibrillar and non-fibrillar elements of the extracellular matrix. The present review highlights recent progress and new insights into biological regulation of extracellular procollagen processing, and some novel functions of byproducts of these extracellular enzymatic transformations. These findings underscore the notion that released pro-peptides and other proteolytic products of extracellular matrix proteins have important biological functions, and that structural proteins are multifunctional. An emerging concept is that a dynamic interplay exists between extracellular products and byproducts with cells that helps to maintain normal cellular phenotypes and tissue integrity.
引用
收藏
页码:927 / 937
页数:11
相关论文
共 104 条
[41]   SELECTIVE BINDING OF ANCHORIN-CII (ANNEXIN-V) TO TYPE-II AND X-COLLAGEN AND TO CHONDROCALCIN (C-PROPEPTIDE OF TYPE-II COLLAGEN) - IMPLICATIONS FOR ANCHORING FUNCTION BETWEEN MATRIX VESICLES AND MATRIX PROTEINS [J].
KIRSCH, T ;
PFAFFLE, M .
FEBS LETTERS, 1992, 310 (02) :143-147
[42]   DEFICIENT PRODUCTION OF LYSYL OXIDASE IN CULTURES OF MALIGNANTLY TRANSFORMED HUMAN-CELLS [J].
KUIVANIEMI, H ;
KORHONEN, RM ;
VAHERI, A ;
KIVIRIKKO, KI .
FEBS LETTERS, 1986, 195 (1-2) :261-264
[43]   Oligomerization-dependent regulation of motility and morphogenesis by the collagen XVIII NC1/endostatin domain [J].
Kuo, CJ ;
LaMontagne, KR ;
Garcia-Cardeña, G ;
Ackley, BD ;
Kalman, D ;
Park, S ;
Christofferson, R ;
Kamihara, J ;
Ding, YH ;
Lo, KW ;
Gillies, S ;
Folkman, J ;
Mulligan, RC ;
Javaherian, K .
JOURNAL OF CELL BIOLOGY, 2001, 152 (06) :1233-1246
[44]   Paired basic/furin-like proprotein convertase cleavage of pro-BMP-1 in the trans-Golgi network [J].
Leighton, M ;
Kadler, KE .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (20) :18478-18484
[45]   The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1 [J].
Li, SW ;
Sieron, AL ;
Fertala, A ;
Hojima, Y ;
Arnold, WV ;
Prockop, DJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (10) :5127-5130
[46]   NMR structure of the netrin-like domain (NTR) of human type I procollagen C-proteinase enhancer defines structural consensus of NTR domains and assesses potential proteinase inhibitory activity and ligand binding [J].
Liepinsh, E ;
Bányai, L ;
Pintacuda, G ;
Trexler, M ;
Patthy, L ;
Otting, G .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (28) :25982-25989
[47]   Elastic fiber homeostasis requires lysyl oxidase-like 1 protein [J].
Liu, XQ ;
Zhao, Y ;
Gao, JG ;
Pawlyk, B ;
Starcher, B ;
Spencer, JA ;
Yanagisawa, H ;
Zuo, J ;
Li, TS .
NATURE GENETICS, 2004, 36 (02) :178-182
[48]   Inactivation of the lysyl oxidase gene Lox leads to aortic aneurysms, cardiovascular dysfunction, and perinatal death in mice [J].
Mäki, JM ;
Räsänen, J ;
Tikkanen, H ;
Sormunen, R ;
Mäkikallio, K ;
Kivirikko, KI ;
Soininen, R .
CIRCULATION, 2002, 106 (19) :2503-2509
[49]   Cloning and characterization of a fourth human lysyl oxidase isoenzyme [J].
Mäki, JM ;
Kivirikko, KI .
BIOCHEMICAL JOURNAL, 2001, 355 (02) :381-387
[50]   Cloning and characterization of a fifth human lysyl oxidase isoenzyme:: the third member of the lysyl oxidase-related subfamily with four scavenger receptor cysteine-rich domains [J].
Mäki, JM ;
Tikkanen, H ;
Kivirikko, KI .
MATRIX BIOLOGY, 2001, 20 (07) :493-496