Akvaporin 1
Akvaporin 1 - bu organizmdagi ko'plab to'qimalarda keng tarqalgan, ayniqsa buyraklarda yuqori darajada ifodalangan suv kanali, akvaporin guruhining oqsilidir .
Tuzilishi va funksiyalari[tahrir | manbasini tahrirlash]
Tuzilishi[tahrir | manbasini tahrirlash]
Akvaporin 1 tetramerik integral oqsil hisoblanadi. Monomer 269 ta aminokislotadan iborat bo'lib, 3 ta transmembran mintaqasi bo'lgan 2 ta tandem takrorini va suv kanalini tashkil etuvchi xarakterli asparagin - prolin - alanin motiviga ega bo'lgan halqani o'zida saqlaydi.
Funksiya[tahrir | manbasini tahrirlash]
Hujayra membranasida, ayniqsa, eritrotsitlar va buyraklarning proksimal kanalchalari hujayralarida o'ziga xos suv kanalini hosil qiladi. Hujayralar membranasi orqali suvning osmotik gradient yo'nalishi bo'yicha harakatini ta'minlab beradi.
To'qimalarda ifodalanishi[tahrir | manbasini tahrirlash]
Akvaporin 1 bir qator to'qimalarda mavjud. Eritrositlarda, buyrak kanalchalari epiteliysida, to'r pardaning pigment epiteliysida, yurak, o'pka, skelet mushaklari, buyrak va oshqozon osti bezida uchraydi. Miya, platsenta va jigarda kam uchraydi.
Koltonning qon guruhi (Co)[tahrir | manbasini tahrirlash]
Akvaporin 1 fragmenti xuddi shu nomdagi qon guruhi uchun mas'ul bo'lgan Kolton antigenidir. Co(a) va Co(b) oqsilining 2ta alleli mavjud bo'lib, odamlarning 99,8 foizida Co(a) alleli mavjud. Akvaporin 1 - Co(AB-) ning to'liq yo'qligi juda kam uchraydi. Koltonning qon guruhi qon quyishda muhim omil hisoblanadi. Ushbu qon guruhi uchun ona va homila o'rtasida nomuvofiqlik bo'lsa, onada homilaning eritrotsitlariga qarshi antitanalarning ishlab chiqarilishi yangi tug'ilgan chaqaloqning gemolitik kasalligiga sabab bo'lishi mumkin.
Manbalar[tahrir | manbasini tahrirlash]
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- Yool A.J., Weinstein A.M. New roles for old holes: ion channel function in aquaporin-1.(ingl.) // Andoza:Нп3 : journal. — 2002. — Andoza:Бсокр. — Andoza:Бсокр. — PMID 11909995.
- Mitra A.K., Ren G., Reddy V.S.,. The architecture of a water-selective pore in the lipid bilayer visualized by electron crystallography in vitreous ice(ingl.) // Novartis Found. Symp. : journal. — 2002. — Andoza:Бсокр. — Andoza:Бсокр. — DOI:10.1002/0470868759.ch4. — PMID 12027013.
- Ripoche P., Goossens D., Devuyst O.,. Role of RhAG and AQP1 in NH3 and CO2 gas transport in red cell ghosts: a stopped-flow analysis(ingl.) // Transfusion clinique et biologique : journal de la Société française de transfusion sanguine : journal. — 2006. — Andoza:Бсокр, Andoza:Бсокр. — Andoza:Бсокр. — DOI:10.1016/j.tracli.2006.03.004. — PMID 16574458.
- Preston G.M., Carroll T.P., Guggino W.B., Agre P. Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein(ingl.) // Science : journal. — 1992. — Andoza:Бсокр, Andoza:Бсокр. — Andoza:Бсокр. — DOI:10.1126/science.256.5055.385. — PMID 1373524.
- Preston G.M., Agre P. Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family(ingl.) // Proceedings of the National Academy of Sciences of the United States of America : journal. — 1992. — Andoza:Бсокр, Andoza:Бсокр. — Andoza:Бсокр. — DOI:10.1073/pnas.88.24.11110. — PMID 1722319.
- Smith B.L., Agre P. Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins(ingl.) // Journal of Biological Chemistry : journal. — 1991. — Andoza:Бсокр, Andoza:Бсокр. — Andoza:Бсокр. — PMID 2007592.
- Denker B.M., Smith B.L., Kuhajda F.P., Agre P. Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules(ingl.) // Journal of Biological Chemistry : journal. — 1988. — Andoza:Бсокр, Andoza:Бсокр. — Andoza:Бсокр. — PMID 3049610.
- Zelinski T., Kaita H., Lewis M.,. The Colton blood group locus. A linkage analysis(aniqlanmagan) // Transfusion. — 1988. — Andoza:Бсокр, Andoza:Бсокр. — Andoza:Бсокр. — DOI:10.1046/j.1537-2995.1988.28588337331.x. — PMID 3166547.
- Preston G.M., Jung J.S., Guggino W.B., Agre P. Membrane topology of aquaporin CHIP. Analysis of functional epitope-scanning mutants by vectorial proteolysis(ingl.) // Journal of Biological Chemistry : journal. — 1994. — Andoza:Бсокр, Andoza:Бсокр. — Andoza:Бсокр. — PMID 7507481.
- Skach W.R., Shi L.B., Calayag M.C.,. Biogenesis and transmembrane topology of the CHIP28 water channel at the endoplasmic reticulum(ingl.) // Andoza:Нп3 : journal. — 1994. — Andoza:Бсокр, Andoza:Бсокр. — Andoza:Бсокр. — DOI:10.1083/jcb.125.4.803. — PMID 7514605.
- Li X., Yu H., Koide S.S. The water channel gene in human uterus(aniqlanmagan) // Biochem. Mol. Biol. Int.. — 1994. — Andoza:Бсокр, Andoza:Бсокр. — Andoza:Бсокр. — PMID 7517253.
- Walz T., Smith B.L., Agre P., Engel A. The three-dimensional structure of human erythrocyte aquaporin CHIP(ingl.) // Andoza:Нп3 : journal. — 1994. — Andoza:Бсокр, Andoza:Бсокр. — Andoza:Бсокр. — PMID 7518771.
- Preston G.M., Smith B.L., Zeidel M.L.,. Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels(ingl.) // Science : journal. — 1994. — Andoza:Бсокр, Andoza:Бсокр. — Andoza:Бсокр. — DOI:10.1126/science.7521540. — PMID 7521540.
- Smith B.L., Preston G.M., Spring F.A.,. Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens(ingl.) // Andoza:Нп3 : journal. — 1994. — Andoza:Бсокр, Andoza:Бсокр. — Andoza:Бсокр. — DOI:10.1172/JCI117418. — PMID 7521882.
- van Hoek A.N., Wiener M.C., Verbavatz J.M.,. Purification and structure-function analysis of native, PNGase F-treated, and endo-beta-galactosidase-treated CHIP28 water channels(ingl.) // Biochemistry : journal. — 1995. — Andoza:Бсокр, Andoza:Бсокр. — Andoza:Бсокр. — DOI:10.1021/bi00007a015. — PMID 7532004.
- Keen T.J., Inglehearn C.F., Patel R.J.,. Localization of the aquaporin 1 (AQP1) gene within a YAC contig containing the polymorphic markers D7S632 and D7S526(ingl.) // Genomics : journal. — 1995. — Andoza:Бсокр, Andoza:Бсокр. — Andoza:Бсокр. — DOI:10.1016/0888-7543(95)80070-3. — PMID 7540589.