机构:
Rutgers State Univ, Dept Pharmacol & Toxicol, Ernest Mario Sch Pharm, Piscataway, NJ 08854 USARutgers State Univ, Dept Pharmacol & Toxicol, Ernest Mario Sch Pharm, Piscataway, NJ 08854 USA
Gordon, Marion K.
[1
]
Hahn, Rita A.
论文数: 0引用数: 0
h-index: 0
机构:
Rutgers State Univ, Dept Pharmacol & Toxicol, Ernest Mario Sch Pharm, Piscataway, NJ 08854 USARutgers State Univ, Dept Pharmacol & Toxicol, Ernest Mario Sch Pharm, Piscataway, NJ 08854 USA
Hahn, Rita A.
[1
]
机构:
[1] Rutgers State Univ, Dept Pharmacol & Toxicol, Ernest Mario Sch Pharm, Piscataway, NJ 08854 USA
Collagens;
Extracellular matrix;
Fibrils;
FACITs;
Basement membrane;
BASEMENT-MEMBRANE ZONE;
VERTEBRATE FIBRILLAR COLLAGEN;
VIII COLLAGEN;
XII COLLAGEN;
V COLLAGEN;
X COLLAGEN;
MACROMOLECULAR ORGANIZATION;
TRANSMEMBRANE PROTEINS;
EPIDERMOLYSIS-BULLOSA;
SULFATE PROTEOGLYCAN;
D O I:
10.1007/s00441-009-0844-4
中图分类号:
Q2 [细胞生物学];
学科分类号:
071009 ;
090102 ;
摘要:
The collagens represent a family of trimeric extracellular matrix molecules used by cells for structural integrity and other functions. The three a chains that form the triple helical part of the molecule are composed of repeating peptide triplets of glycine-X-Y. X and Y can be any amino acid but are often proline and hydroxyproline, respectively. Flanking the triple helical regions (i.e., Col domains) are nonglycine-X-Y regions, termed non-collagenous domains. These frequently contain recognizable peptide modules found in other matrix molecules. Proper tissue function depends on correctly assembled molecular aggregates being incorporated into the matrix. This review highlights some of the structural characteristics of collagen types I-XXVIII.