Biopolym. Cell. 2002; 18(1):57-61.
Structure and Function of Biopolymers
The structure and function of the cotton extensln-like proteins
1Khashimova Z. S., 1Kuznetsova N. N., 1Saitmuratova O. Kh., 1Sadikov A. A.
- A. S. Sadykov Institute of Bioorganic Chemistry
83, Mirzo-Ulugbek Str, Tashkent, Uzbekistan, 100125
Abstract
The structural and functional dependence of the cotton extensin-like proteins (ELPs) has been investigated. ELPs inhibit the cell proliferation, their action depending on the glycoproteins dose and the cell cycle phase. The antiproliferative activity of deglycosylated ELPs towards the KML cell line is higher than that of the extensin-like proteins. The KML cell culture and molecular modelling methods have been used in this work.
Full text: (PDF, in Russian)
References
[1]
Dwek RA. Glycobiology: toward understanding the function of sugars. Chem Rev. 1996;96(2):683-720.
[2]
Lis H, Sharon N. Protein glycosylation. Structural and functional aspects. Eur J Biochem. 1993;218(1):1-27.
[3]
Smith JJ, Muldoon EP, Lamport DTA. Isolation of extensin precursors by direct elution of intact tomato cell suspension cultures. Phytochemistry. 1984;23(6):1233–9.
[4]
Mellon JE, Helgeson JP. Interaction of a hydroxyproline-rich glycoprotein from tobacco callus with potential pathogens. Plant Physiol. 1982;70(2):401-5.
[5]
Weiser RL, Wallner SJ, Waddell JW. Cell Wall and Extensin mRNA Changes during Cold Acclimation of Pea Seedlings. Plant Physiol. 1990;93(3):1021-6.
[6]
Smith JJ, Muldoon EP, Willard JJ, Lamport DTA. Tomato extensin precursors P1 and P2 are highly periodic structures. Phytochemistry. 1986;25(5):1021–30.
[7]
van Holst GJ, Varner JE. Reinforced Polyproline II Conformation in a Hydroxyproline-Rich Cell Wall Glycoprotein from Carrot Root. Plant Physiol. 1984;74(2):247-51.
[8]
Kieliszewski M, Lamport DTA. Cross-reactivities of polyclonal antibodies against extensin precursors determined via elisa techniques. Phytochemistry. 1986;25(3):673–7.
[9]
Khashimova ZS, Mangutova JuS, Suslo ME, Leontjev VB. Hybridomas producing the monoclonal antibodies to the cotton membrane proteins. Biopolym Cell. 1999; 15(4):283-8.
[10]
Lowry Oh, Rosebrough Nj, Farr Al, Randall Rj. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951;193(1):265-75.
[11]
Khashimova ZS, Kuznetsova NN, Mardanova ZI, Leont’ev VB. A study of the mechanism of the action of extensin-like proteins of the cotton plant in a cell culture. Chemistry of Natural Compounds. 1999;35(3):336–8.
[12]
Sharon N, Lis H. Lectins. London; New York: Chapman and Hall, 1985. 114 p.
[13]
Khashimova ZS, Mangutova YS, Suslo MY, Beknazarova DM, Leont’ev VB. Study of the membrane proteins of the cotton plant using monoclonal antibodies. Chemistry of Natural Compounds. 1994;30(1):73–7.
[14]
Nuridzhanyants SS, Kuznetsova IN, Baram NI, Auyelbekov S, Leont'yev VB, Ismailov AI, Aslanov KhA. The cytotoxic activity of gossypol and some of its derivatives. Proc IV All-Union Symposium. by phenolic compounds. Tashkent: FAN, 1982: 33-34.
[15]
Iwamoto Y, Robey FA, Graf J, Sasaki M, Kleinman HK, Yamada Y, Martin GR. YIGSR, a synthetic laminin pentapeptide, inhibits experimental metastasis formation. Science. 1987;238(4830):1132-4.
[16]
Stafstrom JP, Staehelin LA. The role of carbohydrate in maintaining extensin in an extended conformation. Plant Physiol. 1986;81(1):242-6.
[17]
Lamport DTA. Structure and function of plant glycoproteins. The Biochemisty of Plants. Ed. J . Preiss. New York: Acad, press, 1980. Vol. 3: 501-41.
[18]
Hughes RC. Glycoproteins. London ; New York : Chapman and Hall, 1983. 95 p
