Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0403608 (ureter)
 9,655 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An antiserum against human epidermal keratins was used to detect keratins in frozen sections of various rabbit and human tissues by indirect immunofluorescence. Strong staining was observed in all stratified squamous epithelia (epidermis, cornea, conjunctiva, tongue, esophagus, vagina, and anus), in epidermal appendages (hair follicle, sebaceous gland, ductal and myoepithelial cells of sweat glands), as well as in Hassall's corpuscles of the thymus, indicating that all contain abundant keratins. No staining by the antiserum was observed in fibroblasts, muscle of any type, cartilage, blood vessel, nerve tissue, iris or lens epithelium, or the glomerular or tubular cells of the kidney. In contrast, the antiserum stained the cells of most epithelia of the intestinal tract, urinary tract (urethra, bladder, ureter, collecting ducts of kidney), female genital tract (cervix, cervical glands, uterus, and oviduct), and respiratory tract (trachea and bronchi). Epithelial cells of the fine ductal system in the pancreas and submaxillary gland also stained well. When primary cultures of epithelial cells derived from bladder, intestine, kidney, and trachea were grown on glass coverslips and stained with anti-keratin, fiber networks similar to those of cultured keratinocytes were observed. These results show that keratins constitute a cytoskeleton in epithelial cells of diverse morphology and embryological origin. The stability of keratin filaments probably confers the structural strength necessary for cells covering a free surface. Keratin staining can be used to obtain information about the origin of cell lines.
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PMID:Keratin cytoskeletons in epithelial cells of internal organs. 11 Dec 42

The keratins, members of the intermediate filament family, are characteristically expressed in epithelial cells. In the various types of epithelia, the keratin expression pattern is characterized by cell-type specific combinations of the keratin isotypes with a plain pattern in monolayered (simple) epithelia and more complex patterns in stratified and pseudostratified epithelia. Here we demonstrate that the transitional epithelium of the human urinary tract holds an exceptional position between the pseudostratified and stratified epithelia. We show that the simple epithelia keratins 7, 8, 18 and 19 are expressed throughout the whole epithelium as known from pseudostratified epithelia. In addition, we demonstrate expression of keratins 5, 14 and 17, otherwise present in basal cells of multilayered epithelia, and keratins 4 and 13, present in suprabasal areas of non cornified multilayered epithelia. Moreover, we report differences in expression in the various morphological parts of the urinary tract which might be related to their specific functions. Keratin 20, a typical component of the simple epithelia of the digestive tract, is present in bladder and ureter but not in the renal pelvis. Keratin 6, typical for stratified epithelia, is found only in parts of the renal pelvis. We further show that changes in keratin pattern occur during the development from embryonic to adult bladder urothelium. In contrast to adult tissue, the simple type keratins 7, 8 and 18 are not synthesized in basal embryonic cells. Further, keratin 20, present in cells facing the bladder lumen in adult urothelium, is expressed in all but the basal cells in embryonic bladder.
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PMID:Staining patterns of keratins in the human urinary tract. 1976 May 92