دورية أكاديمية
Identification of a specific receptor for interstitial collagenase on osteoblastic cells.
| العنوان: | Identification of a specific receptor for interstitial collagenase on osteoblastic cells. |
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| المؤلفون: | Omura TH; Department of Pharmacological and Physiological Science, St. Louis University School of Medicine, Missouri 63104., Noguchi A, Johanns CA, Jeffrey JJ, Partridge NC |
| المصدر: | The Journal of biological chemistry [J Biol Chem] 1994 Oct 07; Vol. 269 (40), pp. 24994-8. |
| نوع المنشور: | Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print Cited Medium: Print ISSN: 0021-9258 (Print) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology |
| مواضيع طبية MeSH: | Osteoblasts/*chemistry , Receptors, Cell Surface/*analysis, Animals ; Cell Line ; Collagenases/metabolism ; Matrix Metalloproteinase 1 ; Rats |
| مستخلص: | We have previously shown that the rat osteoblastic cell line UMR 106-01 responds to parathyroid hormone treatment by secreting interstitial collagenase. Secreted collagenase reaches a maximal concentration 12-24 h after parathyroid hormone stimulation, but then declines to undetectable levels by 96 h. Neither spontaneous nor cell-mediated extracellular degradation could account for this disappearance, since the enzyme maintained stability in both fresh and conditioned media. Instead, a cell-mediated binding mechanism was suggested by the rapid and saturable removal of exogenous purified rat collagenase at 37 degrees C. Binding studies using 125I-collagenase at 4 degrees C indicated a saturable receptor of a single class and 12,000 receptors per cell (Kd = 5 x 10(-9) M). A time course revealed specific receptor-mediated binding within 10 min and equilibrium by 60 min, while dissociation experiments further demonstrated reversibility. The kinetics of 125I-collagenase binding are characterized by the association (k1 = 4 x 10(6) M-1 min-1) and dissociation (k-1 = 2 x 10(-3) min-1) rate constants. The receptor was shown to be specific for rat collagenase since a host of related and unrelated proteins failed to compete for binding. Internalization studies revealed maximal intracellular accumulation at 30 min and complete degradation by 90 min, suggesting this receptor functions in these osteoblastic cells to eliminate extracellular collagenase. |
| معلومات مُعتمدة: | AR40661 United States AR NIAMS NIH HHS; HD05291 United States HD NICHD NIH HHS |
| فهرسة مساهمة: | Keywords: Non-programmatic |
| المشرفين على المادة: | 0 (Receptors, Cell Surface) EC 3.4.24.- (Collagenases) EC 3.4.24.7 (Matrix Metalloproteinase 1) |
| تواريخ الأحداث: | Date Created: 19941007 Date Completed: 19941104 Latest Revision: 20210212 |
| رمز التحديث: | 20231215 |
| PMID: | 7929184 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 0021-9258 |
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