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1.
The recombinants of the mandibular molar bud epithelia with cranial ectomesenchymal cell groups from several different sources--mandibular molar area, tongue anlagen, and lateral nasal process--were cultured. Dental laminalike buds were developed in each of the recombinants (incidence of development 38-86%). In the heterotrophic recombinants, heterotypic differentiation of mandibular epithelium was also induced. However, the foreign ectomesenchymal cells were not induced heterotypically by the epithelial genetic factor, but the mesenchymal genetic factor is maintained. It is suggested that mandibular molar bud epithelia have potency to proliferate into mesenchyme under non-organ-specific influences of ectomesenchymal cells and that presumptive mandibular mucosal epithelia have multipotency for differentiation sensitive to inductive influences by the heterotypic cranial ectomesenchymal cells but that the mandibular molar bud epithelia have no heterotypic inductive activity for the differentiation of cranial ectomesenchymal cells. 相似文献
2.
S Tsuzuki T Fushiki A Kondo H Murayama E Sugimoto 《European journal of biochemistry》1991,199(1):245-252
The adaptation to a high protein diet of the concentration and mRNA level of a trypsin-sensitive, cholecystokinin-releasing peptide (monitor peptide), which was proposed to be the mediator of the cholecystokinin release in response to protein intake, was investigated in the rat pancreas. Adult rats were placed on one of two isocaloric diets. One group was fed a 22% casein diet (control diet) and the other a 64% casein diet (high-protein diet) for 14 days. In order to quantify the monitor peptide separately from pancreatic secretory trypsin inhibitor (PSTI-II), which is highly similar in its amino acid and mRNA nucleotide sequences to the monitor peptide but has less cholecystokinin-releasing activity, we used specific assay methods: HPLC was used for determining the monitor peptide concentration in zymogen granules and a synthetic oligonucleotide probe for determining the mRNA of the monitor peptide in the pancreas. The concentrations in the zymogen granules and the mRNA levels in the pancreas of the two peptides increased in parallel during the adaptation to the high protein diet, indicating that these two peptides were under the same control during the adaptation. The concentration and mRNA level of the monitor peptide, which were measured after 0, 3, and 14 days, increased throughout the experiment period, as did the concentration of trypsin. This suggested that the monitor peptide and trypsin may respond to similar signals during the adaptation to a high protein diet and that this apparent coordination may facilitate the adaptation of the pancreas to the diet. 相似文献
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Kazuyuki Morihara Tatsushi Oka Hiroshige Tsuzuki 《Bioscience, biotechnology, and biochemistry》2013,77(9):836-839
Relation between the elastolytic and depilatory activities was examined using various highly purified proteinase preparations. Elastolytic activity of the enzymes did not correlates well with their depilatory action. Among 11 proteinase preparations tested, Pseudomonas aeruginosa elastase showed the highest depilatory activity. 相似文献
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Miyata Seiko Otake Hironao Fujishiro Hiroshige Iwamoto Kunihiro Noda Akiko Sone Michihiko Ozaki Norio 《Sleep and biological rhythms》2022,20(3):403-411
Sleep and Biological Rhythms - Sleep problems and obstructive sleep apnea (OSA) increase with age and disturb life in old age. Positional therapy is one option to treat OSA, but the differences in... 相似文献
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Nobuhito Murai Yuka Miyake Satoshi Tsuzuki Kuniyo Inouye Tohru Fushiki 《Cytotechnology》2009,59(3):169-176
Matriptase is a type II transmembrane serine protease. This protease is strongly expressed in simple epithelial cells such
as enterocytes and kidney tubular cells in which the plasma membranes are separated into apical and basolateral domains. Although
matriptase was found previously to occur exclusively on the basolateral membrane of enterocytes, the underlying mechanism
of localization is unclear. In the present study, a full-length rat matriptase and a chimera consisting of the cytoplasmic
and transmembrane regions of the protease and green fluorescent protein (designated as 1–86GFP) were found to localize exclusively
to the basolateral membrane domain when expressed in Madin–Darby canine kidney epithelial cells. Mutagenesis analysis of 1–86GFP
revealed that the matriptase cytoplasmic juxtamembrane amino acid residues (Lys45, Val47, and Arg50) play a role in mediating
the localization in the cells. This study provides the first evidence that matriptase carries information for its localization
in simple epithelia. 相似文献
10.
Yuka Miyake Satoshi Tsuzuki Makoto Yasumoto Tohru Fushiki Kuniyo Inouye 《Cytotechnology》2009,60(1-3):95-103
Hepatocyte growth factor activator inhibitor type I (HAI-1) is a membrane-bound, serine protease inhibitor with two protease-inhibitory domains (Kunitz domain I and II). HAI-1 is known as a physiological inhibitor of a membrane-bound serine protease, matriptase. Paradoxically, however, HAI-1 has been found to be required for the extracellular appearance of the protease in an expression system using a monkey kidney COS-1 cell line. In the present study, we show using COS-1 cells that co-expression of recombinant variants of HAI-1 with the inhibition activity toward matriptase, including a variant consisting only of Kunitz domain I (the domain responsible for inhibition of matriptase), allowed for the appearance of this protease in the conditioned medium, whereas that of the variants without the activity did not. These findings suggest that the inhibition activity toward matriptase is critical for the extracellular appearance of protease in COS-1 cells. 相似文献