Oh S P, Griffith C M, Hay E D, Olsen B R
Department of Anatomy and Cellular Biology, Harvard Medical School, Boston, Massachusetts 02115.
Dev Dyn. 1993 Jan;196(1):37-46. doi: 10.1002/aja.1001960105.
Polyclonal antibodies were raised in rabbits against a fusion peptide representing a portion of the amino-terminal non-triple-helical domain of mouse type XII collagen. The antibodies reacted with bands of 220 and 350 kDa on Western blots of mouse tissue extracts. Immunohistochemical analyses of mouse embryos demonstrated that type XII collagen is expressed mainly in dense connective tissues of tendons, ligaments, dermis, cornea, blood vessel walls, meninges, and developing membranous bones. Comparison of skin extracts and medium of cultured mouse skin fibroblasts by Western blotting showed that while tissue contain short 220 kDa type XII collagen polypeptides as well as the long form, cultured cells produce mainly the long form with 350 kDa polypeptides.
针对代表小鼠Ⅻ型胶原蛋白氨基末端非三螺旋结构域一部分的融合肽，在兔体内制备了多克隆抗体。这些抗体在小鼠组织提取物的蛋白质免疫印迹上与220 kDa和350 kDa的条带发生反应。对小鼠胚胎的免疫组织化学分析表明，Ⅻ型胶原蛋白主要表达于肌腱、韧带、真皮、角膜、血管壁、脑膜和正在发育的膜性骨的致密结缔组织中。通过蛋白质免疫印迹对培养的小鼠皮肤成纤维细胞的皮肤提取物和培养基进行比较显示，虽然组织中含有短的220 kDaⅫ型胶原蛋白多肽以及长形式，但培养的细胞主要产生具有350 kDa多肽的长形式。
