Primary structure of tetranectin, a plasminogen kringle 4 binding plasma protein: homology with asialoglycoprotein receptors and cartilage proteoglycan core protein

Biochemistry ◽  
1987 ◽  
Vol 26 (21) ◽  
pp. 6757-6764 ◽  
Author(s):  
Jannie Fuhlendorff ◽  
Inge Clemmensen ◽  
Staffan Magnusson
1987 ◽  
Vol 262 (36) ◽  
pp. 17757-17767 ◽  
Author(s):  
K Doege ◽  
M Sasaki ◽  
E Horigan ◽  
J R Hassell ◽  
Y Yamada

1979 ◽  
Vol 11 (1) ◽  
pp. 253-259 ◽  
Author(s):  
Christine Mercier-Bodard ◽  
Jack-Michel Renoir ◽  
Etienne-Emile Baulieu

1991 ◽  
Vol 25 (3-4) ◽  
pp. 311-320 ◽  
Author(s):  
Stephen E. Haynesworth ◽  
David A. Carrino ◽  
Arnold I. Caplan

1988 ◽  
Vol 95 (1) ◽  
pp. 169-176 ◽  
Author(s):  
E.R. Pettipher ◽  
B. Henderson ◽  
S. Moncada ◽  
G.A. Higgs

1984 ◽  
Vol 106 (3) ◽  
pp. 428-432 ◽  
Author(s):  
Yoshiyuki Maruyama ◽  
Norihiko Aoki ◽  
Yasuyuki Suzuki ◽  
Hyogo Sinohara ◽  
Toshio Yamamoto

Abstract. A radioimmunoassay for human sex-steroidbinding plasma protein (SBP) was developed. With this assay, SBP was determined in sera of 138 normal men and 169 non-pregnant women, ranging in age from 11 to 87 years. The results indicate (i) that SBP levels in both sexes increase gradually with age up to mid-eighties, (ii) that the average levels in mid-eighties are approximately twice those in early twenties, and (iii) that the average levels in women are about twice as high as those in men of corresponding age. These results may also account for the discrepancies in the previous papers regarding the normal blood levels and sexual difference of SBP in adult men and women.


1993 ◽  
Vol 7 (2) ◽  
pp. 100-104 ◽  
Author(s):  
Yuji Hinoda ◽  
Yoshiaki Arimura ◽  
Fumio Itoh ◽  
Masaaki Adachi ◽  
Masayuki Tsujisaki ◽  
...  

1986 ◽  
Vol 236 (1) ◽  
pp. 71-75 ◽  
Author(s):  
T T Glant ◽  
K Mikecz ◽  
P J Roughley ◽  
E Buzás ◽  
A R Poole

Monoclonal antibodies were prepared that recognize different age-related epitopes on proteoglycan subunits of high buoyant density isolated from human epiphysial and articular cartilages. Antibody EFG-4 (IgG1) recognizes a proteinase-sensitive segment associated with the core protein. Antibody BCD-4 (IgG1) reacts with keratan sulphate bound to core protein. Both epitopes are minimally expressed in foetal cartilage and increase with age after birth to become maximally expressed in adult cartilage by about 30 years of age. In contrast, monoclonal antibody alpha HFPG-846 (IgM) recognizes a core-protein-related epitope that is maximally expressed in young foetal cartilage, declines up to birth and thereafter and is almost absent after about 30 years of age. Antibody alpha HFPG-846 was used to isolate by immuno-affinity chromatography two subpopulations of proteoglycan subunits from a 16-year-old-human cartilage proteoglycan subunit preparation. Only the antibody-unbound population showed a significant reaction with antibodies EGF-4 and BCD-4. The amino acid and carbohydrate compositions of these proteoglycan fractions were different, and one (antibody-bound) resembled those of foetal and the other (antibody-unbound) resembled those of adult proteoglycans isolated from 24-27-week-old-foetal and 52-56-year-old-adult cartilage respectively. These observations demonstrate that human cartilages contain at least two chemically and immunochemically distinct populations of proteoglycans, the proportions and content of which are age-dependent. It is likely that these populations represent the products of different genes, though their heterogeneity may be compounded by the result of different post-translation modifications.


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