183:
C-lectin domains. From this mannose family, collagen is specifically bound by mannose receptor, M-phospholipase A2 receptor and Endo180 receptor. Binding of collagen or denatured collagen (gelatin) is provided by F2 domain and partly by C-terminal domain (aa 1000-1453), which binds type I collagen triple helix. Inability to internalize collagen and reduced ability of adhesion and related increased migration in collagen matrix was observed in fibroblast population with nonfunctional Endo180 receptor. The exact principal of collagen binding to mannose receptor is not known so far. Endo180 receptor is expressed on fibroblasts, endothelial cells and macrophages.
134:. The exact way of receptor activation is unknown so far. Unlike other tyrosine-kinase receptors, maximal activation of receptors occurs 18 hours after collagen stimulation. They function as receptors for different collagen types, they recognize many fibrillar collagens and they are capable of binding some nonfibrillar collagens as well. Nevertheless, the native conformation of collagen is a requirement for receptor binding, denatured collagen is not bound. DDRs are expressed widely already during development and level of expression is high in adults as well.
165:
belongs to collagen receptors that are primarily expressed on platelets surface. Together with integrin receptor α2β1 they provide coagulation cascade activation when a blood-vessel is damaged. When damage occurs, endothelial collagen is uncovered and is bound by GPVI receptor on platelets. This interaction activates signalling cascades leading to coagulation factors release. Mainly fibrillar collagens type I and III serve as ligands. Functions include: Platelet adhesion and activation - the most important platelet collagen receptor in terms of signaling.
171:(Leukocyte-associated IG-like receptor) works as inhibition signal for different immune cells. Lair-1 consists of Ig domain, transmembrane helix and a short cytosolic domain, which includes two inhibition motifs (ITIMs), which can block tyrosine domain when activated. A ligand of Lair-1 receptor is type XVII transmembrane collagen, it binds type I and III collagen as well. Collagen binding inhibits Lair-1 function.
114:
is expressed by mesenchymal cells in some parts of embryo during its development and also in muscles in adults: it preferably binds fibrillar collagen. Integrin receptors capable of collagen binding could, according to results of (Garnotel R et al. 2000), include integrin α10β2, which is situated on
164:
with ITAM (immunoreceptor tyrosine-based activation motif) domain is associated with the transmembrane domain. The short cytosolic domain interacts with calmodulin and Src kinases Lyn and Fyn. These Src kinases phosphorylate tyrosine in ITAM domain and activate a signalling cascade. Glycoprotein VI
147:
structure as above. Binds fibril-forming collagens, collagen of types I, II, III and X. A specific binding site in collagen II has been identified. It is specific for mesenchymal cells. Functions include: Chondrocyte proliferation and bone growth; regulation of cell proliferation, cell adhesion and
159:
Receptor GPVI belongs to immunoglobulin family of glycoproteins. It consists of two extramembrane immunoglobulin domains, which are associated with extracellular glycosylated mucine and together they form a stalk. Another part of the receptor consists of transmembrane helix with a short cytosolic
140:
is a homodimer. Its ectodomain consists of a collagen-binding discoidin domain followed by ~200 residues of unknown structure. It binds fibril-forming collagens and primarily type IV collagen, but also collagen of types I, VI, VIII. It is expressed mainly in epithelial cells and leukocytes and
182:
provide reception of extracellular ligands. To the family of mannose receptors belong: mannose receptor, M-phospholipase A2 receptor (PLA2R), Dec-205, Endo180/uPARAP. They share and extracellular domain, which contains N-terminal domain rich in cystein, F2 fibronectin type II domain and several
86:
binds to collagen via the MIDAS motif in the α subunit I domain. It preferentially binds collagens IV, VI and type XIII collagen, but also fibril-forming collagens. Specific binding sites in collagen I and IV have been identified. This receptor is situated mainly on mesenchymal cells. Functions
97:
preferentially binds fibril-forming collagens. Specific binding sites in collagen I and III have been identified. Integrin α2β1 is expressed mainly on epithelial cells and platelets. Functions include: platelet adhesion - the most abundant receptor for collagen in
141:
expression rate changes due to cell cycle phase. Functions include: mammary gland development; arterial wound repair; regulation of cell proliferation, cell adhesion and MMP expression; kidney function, differentiation and function of leukocytes.
79:
function as the major cell receptor for extracellular matrix protein. These receptors comprise an α and β transmembrane subunit, which are noncovalently bound. Collagen binding is primarily provided by integrins α1β1, α2β1, α10β1 and α11β1.
130:. Receptor activation happens when collagen binds into preformed DDR dimers on cell membrane, when collagen is bound, a conformational change probably occurs, which causes cytosolic kinases to rotate to face each other, and their
26:, the most abundant protein in mammals. They control mainly cell proliferation, migration and adhesion, coagulation cascade activation and they affect ECM structure by regulation of MMP (matrix metalloproteinases).
292:
White, D.J., Puranen, S., Johnson, M.S., Heino, J., 2004. The collagen receptor subfamily of the integrins. International
Journal of Biochemistry & Cell Biology 36, 1405-1410.
108:
preferentially binds collagens IV and VI, but also collagen II. It is expressed on chondrocytes and cardiac muscle. Involved in growth plate morphogenesis and function.
144:
309:
253:"Glycoprotein VI is the collagen receptor in platelets which underlies tyrosine phosphorylation of the Fc receptor gamma-chain"
37:
65:
102:; branching morphogenesis; mast cell activation; keratinocyte adhesion and it is the main regulator of cell migration.
289:
Vogel, W.F., 2001. Collagen-receptor signaling in health and disease. European
Journal of Dermatology 11, 506-514.
203:
127:
123:
88:
53:
111:
105:
131:
94:
83:
304:
161:
274:
233:
41:
199:
264:
225:
179:
156:
269:
252:
298:
229:
76:
64:. The leading role in the elimination of high-stress injury is taken by the
237:
278:
99:
61:
57:
23:
216:
Leitinger B, Hohenester E (April 2007). "Mammalian collagen receptors".
87:
include: fibroblast proliferation; regulation of collagen synthesis and
251:
Gibbins JM, Okuma M, Farndale R, Barnes M, Watson SP (August 1997).
168:
22:
are membrane proteins that bind the extracellular matrix protein
137:
49:
45:
29:There are at least eight human collagen receptors.
8:
268:
202:at the U.S. National Library of Medicine
192:
91:expression; response to renal injury.
115:monocytes and binds type I collagen.
7:
14:
38:Platelet membrane glycoproteins
33:Platelet membrane glycoproteins
1:
270:10.1016/S0014-5793(97)00926-5
152:Immunoglobulin-like receptors
148:induction of MMP expression.
230:10.1016/j.matbio.2006.10.007
66:glycoprotein Ib-IX-V complex
326:
124:Discoidin domain receptors
119:Discoidin domain receptors
128:receptor tyrosine kinases
204:Medical Subject Headings
310:Cell adhesion proteins
16:Cell surface receptors
52:as well, function as
56:engaged in platelet
132:autophosphorylation
126:form a subgroup of
20:Collagen receptors
200:Collagen+Receptor
175:Mannose receptors
317:
283:
282:
272:
248:
242:
241:
213:
207:
197:
180:Mannose receptor
325:
324:
320:
319:
318:
316:
315:
314:
295:
294:
287:
286:
250:
249:
245:
215:
214:
210:
198:
194:
189:
177:
157:Glycoprotein VI
154:
121:
74:
35:
17:
12:
11:
5:
323:
321:
313:
312:
307:
297:
296:
285:
284:
243:
208:
191:
190:
188:
185:
176:
173:
153:
150:
120:
117:
112:Integrin α11β1
106:Integrin α10β1
73:
70:
34:
31:
15:
13:
10:
9:
6:
4:
3:
2:
322:
311:
308:
306:
303:
302:
300:
293:
290:
280:
276:
271:
266:
262:
258:
254:
247:
244:
239:
235:
231:
227:
224:(3): 146–55.
223:
219:
212:
209:
205:
201:
196:
193:
186:
184:
181:
174:
172:
170:
166:
163:
158:
151:
149:
146:
142:
139:
135:
133:
129:
125:
118:
116:
113:
109:
107:
103:
101:
96:
95:Integrin α2β1
92:
90:
85:
84:Integrin α1β1
81:
78:
71:
69:
67:
63:
59:
55:
51:
48:and probably
47:
43:
39:
32:
30:
27:
25:
21:
291:
288:
263:(2): 255–9.
260:
256:
246:
221:
217:
211:
195:
178:
167:
155:
143:
136:
122:
110:
104:
93:
82:
75:
36:
28:
19:
18:
218:Matrix Biol
299:Categories
187:References
162:FcRγ chain
160:domain. A
305:Receptors
257:FEBS Lett
100:platelets
77:Integrins
72:Integrins
54:receptors
40:, mainly
238:17141492
62:collagen
58:adhesion
42:GPIa/IIa
24:collagen
279:9280292
277:
236:
206:(MeSH)
169:LAIR1
275:PMID
234:PMID
145:DDR2
138:DDR1
50:GPIV
46:GPVI
265:doi
261:413
226:doi
89:MMP
60:to
301::
273:.
259:.
255:.
232:.
222:26
220:.
68:.
44:,
281:.
267::
240:.
228::
Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.