کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10913977 | 1088685 | 2005 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Pro-α3(V) collagen chain is expressed in bone and its basic N-terminal peptide adheres to osteosarcoma cells
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کلمات کلیدی
PBSDMEMIPTGGSTRT-PCRDulbecco's modified Eagle's medium - Medal of Eagle اصلاح شده DulbeccoHeparin binding - اتصال هپارینisopropyl-β-d-thiogalactopyranoside - ایزوپروپیل-ب-دی-تیوگالکتوپیرانوزیدGene expression - بیان ژنELISA - تست الیزاEnzyme-linked immunosorbent assay - تست الیزاBone formation - تشکیل استخوان Phosphate-buffered saline - محلول نمک فسفات با خاصیت بافریreverse transcription-polymerase chain reaction - واکنش زنجیره ای رونویسی-پلیمراز معکوسglutathione S-transferase - گلوتاتیون S-ترانسفراز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
تحقیقات سرطان
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Pro-α3(V) collagen chain is expressed in bone and its basic N-terminal peptide adheres to osteosarcoma cells Pro-α3(V) collagen chain is expressed in bone and its basic N-terminal peptide adheres to osteosarcoma cells](/preview/png/10913977.png)
چکیده انگلیسی
The third α-chain of type V collagen, α3(V) chain, was initially identified in the placenta more than 20 years ago, but was poorly characterized with regard to its expression and function. We generated a specific monoclonal antibody against the N-terminal domain of the pro-α3(V) chain and examined gene expression using immunohistochemical methods combined with in situ hybridization. The pro-α3(V) chain was seen in funis and amnion, but not chorionic villi and deciduas of mouse placenta. In mouse embryo, the transcripts of the pro-α3(V) gene were seen in tissues that were related to bone formation as well as developing muscle and nascent ligament previously reported (J. Biol. Chem. 275, 8749-8759, 2000). However, immunohistochemistry showed that pro-α3(V) protein accumulated rather in the developing bone of mouse embryo. On the other hand, the N-terminal globular domain of the pro-α3(V) chain has a unique structure that contains a highly basic segment of 23 amino acids. The peptide derived from the basic segment showed a specific adhesive feature to osteosarcoma cells but not to chondrosarcoma cells. The four heparin binding sites in the basic segment equally contribute toward adhesion to the osteosarcoma cells. Our data suggested that N-terminal globular domain of the pro-α3(V) chain influence bone formation of osteoblasts through proteoglycan on the cell surface during development or regeneration.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Matrix Biology - Volume 24, Issue 4, June 2005, Pages 283-294
Journal: Matrix Biology - Volume 24, Issue 4, June 2005, Pages 283-294
نویسندگان
Kenji Yamaguchi, Noritaka Matsuo, Hideaki Sumiyoshi, Noritaka Fujimoto, Ken-ich Iyama, Shigetaka Yanagisawa, Hidekatsu Yoshioka,