Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Most.Nahid Parvin"'
Autor:
Hiroshi Yamashita, Keiko Tsumura, Kiyotoshi Inenaga, Most.Nahid Parvin, Xuefei Li, Tetsuya Akamatsu, Norio Kanamori, Chenjuan Yao, Kazuo Hosoi, Kwartarini Murdiastuti
Publikováno v:
American Journal of Physiology-Renal Physiology. 290:F478-F485
Aquaporin-2 (AQP2) is responsible for the concentration of urine in the kidney collecting tubule under the regulation of vasopressin. The mRNA level of this water channel in polydipsic STR/N mice was extremely reduced compared with that in normal ICR
Autor:
Kazuo Hosoi, Norio Kanamori, Chisato Kosugi-Tanaka, Tetsuya Akamatsu, Kwartarini Murdiastuti, Most.Nahid Parvin, Osamu Miki, Chenjuan Yao
Publikováno v:
Pflügers Archiv - European Journal of Physiology. 446:641-651
The expression and localization of aquaporins (AQP1-AQP5), members of the water channel family, in the developing rat submandibular gland were analysed using RT-PCR, Northern blotting and immunohistochemistry to explore their relation to the developm
Autor:
Keiko Tsumura, Tetsuya Akamatsu, K Suzuki, Most.Nahid Parvin, Kazuo Hosoi, Jun Tada, S Matsuura, Wei Wei, Norio Kanamori
Publikováno v:
Immunology. 101:531-540
The connective tissue-type mast cells present in the submandibular gland (SMG) and peritoneal cavity of rats were found to express kininogens (KGs), the expression of which was demonstrated by Western blotting, reverse transcription-polymerase chain
Autor:
Masayuki Shono, Jun Tada, Most.Nahid Parvin, Naoki Yamanaka, Keio Tsumura, Norio Kanamori, Tetsuya Akamatsu, Kazuo Hosoi, Takamasa Sawa
Publikováno v:
Biochemical and Biophysical Research Communications. 266:443-447
A cDNA of rat aquaporin 5 (AQP5) was used to transfect to HSG (human salivary gland cells), and the trafficking mechanism was studied in vitro by confocal laser microscopy. The trafficking of AQP5 to the plasma membrane was induced by stimulation of
Autor:
Norio Kanamori, Chisato Kosugi-Tanaka, Chenjuan Yao, Tetsuya Akamatsu, Kazuo Hosoi, Shingo Kurabuchi, Most.Nahid Parvin, Kwartarini Murdiastuti
Publikováno v:
American journal of physiology. Gastrointestinal and liver physiology. 288(6)
Aquaporin (AQP)5, an exocrine-type water channel, was detected in the rat duodenum by Western blot analysis, and was localized by immunohistochemistry in the secretory granule membranes as well as in the apical and lateral aspects of the plasma membr
Autor:
Chisato Kosugi-Tanaka, Kazuo Hosoi, Osamu Miki, Tetsuya Akamatsu, Kwartarini Murdiastuti, Norio Kanamori, Chenjuan Yao, Most.Nahid Parvin
Publikováno v:
Pflugers Archiv : European journal of physiology. 445(3)
By Western blot analysis, the expression level of aquaporin (AQP) 5 in the submandibular gland (SMG) was found to be different among individual rats of the Sprague-Dawley (SD) strain. Such differences were observed for AQP5 but not for AQP1 and conse
Autor:
Keiko Tsumura, Jun Tada, Wei Wei, Most.Nahid Parvin, Tetsuya Akamatsu, Kazuo Hosoi, Norio Kanamori
Publikováno v:
Life sciences. 69(3)
The mRNAs for acute-phase proteins and kininogens were found to be increased in the submandibular gland (SMG) and extraorbital and intraorbital lacrimal gland (ELG and ILG) in response to experimentally induced inflammation in rats; i.e., 24 hours af
Autor:
Most.Nahid Parvin, Keiko Tsumura, Jun Tada, Yoshiko Matsuda, Kazuo Hosoi, Tetsuya Akamatsu, Norio Kanamori
Publikováno v:
Scopus-Elsevier
The temporospatial expression of PACE4, a member of the mammalian subtilisin-like proprotein convertase family, in the developing rat molar tooth was determined by in situ hybridization. At the initiation stage of tooth development, PACE4 mRNA was we
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. (1-3):116-124
The expression, localization, and regulation of aquaporin 5 (AQP5), a member of the water channel family of proteins, was investigated in tissues of the rat gastrointestinal tract. Reverse transcriptase–polymerase chain reaction (RT–PCR) detected