WordNet

the ratio of the circumference to the diameter of a circle; approximately equal to 3.14159265358979323846...
the 16th letter of the Greek alphabet
the inner part of an organ or structure in plant or animal

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〈C〉パイ(ギリシア語アルファベットの第16字Π,π;英語のP,pに相当) / 〈U〉円周率(記号はπ)
ごちゃまぜの活字 / ごちゃまぜ,混乱
〈U〉骨髄 / =medulla oblongata
《集合的に》たくさんのくい / たくさんのくいで作った物

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1. 脱毛の評価および診断 evaluation and diagnosis of hair loss
2. 化学療法による脱毛 chemotherapy induced alopecia
3. 尿路感染症における細菌付着およびその他の病原因子 bacterial adherence and other virulence factors for urinary tract infection
4. 肺炎桿菌感染症の微生物学および病因 microbiology and pathogenesis of klebsiella pneumoniae infection
5. 髄膜炎菌の微生物学および病理生物学 microbiology and pathobiology of neisseria meningitidis

English Journal

Peptidylarginine deiminase isoforms are differentially expressed in the anagen hair follicles and other human skin appendages.

Nachat R1, Méchin MC, Charveron M, Serre G, Constans J, Simon M.Author information 1CNRS-University of Toulouse III UMR 5165 Epidermis differentiation and rheumatoid autoimmunity, Institut Fédératif de Recherche 30 (INSERM; CNRS; Centre Hospitalier Universitaire de Toulouse; Université Paul Sabatier), Toulouse Cedex, France.AbstractPeptidylarginine deiminases (PAD) catalyze the conversion of arginine residues to citrullines. Five isoforms are known that present distinct tissue locations. In the epidermis, like in the skin, only PAD1, 2, and 3 are expressed. Their pattern of expression in skin appendages is not known. Here, confocal microscopy analysis using highly specific antibodies demonstrated that PAD1 and 3 are expressed in human anagen hair follicles, PAD1 and 2, in arrector pili muscles and sweat glands, whereas no PAD were detected in sebaceous glands. PAD1 was detected in the cuticle and the Huxley layer of the inner root sheath (IRS), and in the companion layer. PAD3 was localized in the medulla, and in the three layers of the IRS. Using anti-modified citrulline antibodies, we also showed that deiminated proteins appeared in the lower part of the IRS, first in the Henle layer, then in the cuticle, and finally in the Huxley layer. Our data demonstrate that PAD3 is the enzyme that deiminates trichohyalin in the medulla and the Henle layer, indicate that PAD1 and 3 are involved in the hair follicle program of differentiation, and suggest a role for PAD1 and 2 in the physiology of sweat glands and arrector pili muscles.
The Journal of investigative dermatology.J Invest Dermatol.2005 Jul;125(1):34-41.
Peptidylarginine deiminases (PAD) catalyze the conversion of arginine residues to citrullines. Five isoforms are known that present distinct tissue locations. In the epidermis, like in the skin, only PAD1, 2, and 3 are expressed. Their pattern of expression in skin appendages is not known. Here, con
PMID 15982300

Variation of high mannose chains of Tamm-Horsfall glycoprotein confers differential binding to type 1-fimbriated Escherichia coli.

Cavallone D1, Malagolini N, Monti A, Wu XR, Serafini-Cessi F.Author information 1Department of Experimental Pathology, University of Bologna, Bologna 40126, Italy.AbstractTamm-Horsfall glycoprotein (THP), the most abundant protein in mammalian urine, has been implicated in defending the urinary tract against infections by type 1-fimbriated Escherichia coli. Recent experimental evidence indicates that the defensive capability of THP relies on its single high mannose chain, which binds to E. coli FimH lectin and competes with mannosylated uroplakin receptors on the bladder surface. Here we describe several major differences, on both structural and functional levels, between human THP (hTHP) and pig THP (pTHP). pTHP contains a much higher proportion (47%) of Man5GlcNAc2 than does hTHP (8%). FimH-expressing E. coli adhere to monomeric pTHP at an approximately 3-fold higher level than to monomeric hTHP. This suggests that the shorter high mannose chain (Man5GlcNAc2) is a much better binder for FimH than the longer chains (Man6-7GlcNAc2) and that pTHP is a more potent urinary defense factor than hTHP. In addition, unlike hTHP whose polyantennary glycans are exclusively capped by sialic acid and sulfate groups, those of pTHP are also terminated by Galalpha1,3Gal epitope. This is consistent with the fact that the outer medulla of pig kidney expresses the alpha1,3-galactosyltransferase, which is completely absent in human kidney. Finally, pTHP is more resistant to leukocyte elastase hydrolysis than hTHP, thus explaining why pTHP is much less prone to urinary degradation than hTHP. These results demonstrate for the first time that the species variations of the glycomoiety of THP can lead to the differential binding of THP to type 1-fimbriated E. coli and that the differences in high mannose processing may reflect species-specific adaptation of urinary defenses against E. coli infections.
The Journal of biological chemistry.J Biol Chem.2004 Jan 2;279(1):216-22. Epub 2003 Oct 21.
Tamm-Horsfall glycoprotein (THP), the most abundant protein in mammalian urine, has been implicated in defending the urinary tract against infections by type 1-fimbriated Escherichia coli. Recent experimental evidence indicates that the defensive capability of THP relies on its single high mannose c
PMID 14570881

Keratin 17 expression in the hard epithelial context of the hair and nail, and its relevance for the pachyonychia congenita phenotype.

McGowan KM1, Coulombe PA.Author information 1Departments of Biological Chemistry and Dermatology, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.AbstractThe hard-keratin-containing portion of the murine hair shaft displays a positive immunoreactivity with an antibody against the soft epithelial keratin, K17. The K17-expressing cell population is located in the medulla compartment of the hair. Consistent with this observation, K17-containing cells also occur in the presumptive medulla precursor cells located in the hair follicle matrix. Western blot analysis of hair extracts prepared from a number of mouse strains confirms this observation and suggests that K17 expression in the hair shaft is a general trait in this species. The expression of K17 in human hair extracts is restricted to eyebrow and facial hair samples. These are the major sites for the occurrence of the pili torti (twisted hair) phenotype in the type 2 (Jackson-Lawler) form of pachyonychia congenita, previously shown to arise from inherited K17 mutations. Given that all forms of pachyonychia congenita show an involvement of the nail, we compared the expression of the two other genes mutated in pachyonychia congenita diseases, K6 and K16, with that of K17 in human nail. All three keratins are abundantly expressed within the nail bed epithelium, whereas K17 protein is expressed in the nail matrix, which contains the epithelial cell precursors for the nail plate. Our data suggest a role for K17 in the formation and maintenance of various skin appendages and directly support the concept that pachyonychia congenita is a disease of the nail bed.
The Journal of investigative dermatology.J Invest Dermatol.2000 Jun;114(6):1101-7.
The hard-keratin-containing portion of the murine hair shaft displays a positive immunoreactivity with an antibody against the soft epithelial keratin, K17. The K17-expressing cell population is located in the medulla compartment of the hair. Consistent with this observation, K17-containing cells al
PMID 10844551