STUDY OF PLASMA LEVELS OF ADIPONECTIN AND RESISTIN IN PATIENTS WITH ESSENTIAL HYPERTENSION
Ahmed Mohamed Moghazy;
Abstract
Discovery:
Adiponectin (ADPN) is an adipocytokine which was identified and named by four independent groups a decade ago. Mouse adiponectin was firstly discovered in 1995 by Scherer's group (I)' who called it adipocyte complement-related protein of 30 KDa (Acrp30), in a subtractive hybridization screen comparing 3T3-Ll adipocytes with undifferentiated preadipocytes. The mRNA was induced over I 00-fold during differentiation and was expressed exclusively in adipocytes.(IJ Adiponectin was also
independently cloned and named adipo Q by Hu et al. ( 2) The human homologue of
adiponectin (which shares 83% similarity with mouse polypeptide) was originally cloned from adipose tissue and named adipose most abundant gene transcript I (apM-1 ). (3) Finally, a very different approach was employed by Nakano and colleagues (4 l, who
isolated adiponectin from human plasma by virtue of its affinity for gelatin, naming it gelatin-binding protein of 28 KDa (GBP28).
Structure:
Mouse adiponectin is a 30 KDa secreted protein and contains 247 amino acids( 5l,
whereas human adiponectin is a 244 amino acids protein of approximately 28 KDa, which belongs to the complement factor C I q family of proteins. 0 l It contains a 20
residue signal peptide at the amino-terminus; a short non-helical, variable region that show no homology among different species; collagen repeats involved in collagen- triple helix formation; and a globular head at the carboxyl terminus, which shows a very high degree of homology with subunits of C1q and the globular domains of type VIII and type
X collagens(4, S) (Figure: I). (6)
Adiponectin (ADPN) is an adipocytokine which was identified and named by four independent groups a decade ago. Mouse adiponectin was firstly discovered in 1995 by Scherer's group (I)' who called it adipocyte complement-related protein of 30 KDa (Acrp30), in a subtractive hybridization screen comparing 3T3-Ll adipocytes with undifferentiated preadipocytes. The mRNA was induced over I 00-fold during differentiation and was expressed exclusively in adipocytes.(IJ Adiponectin was also
independently cloned and named adipo Q by Hu et al. ( 2) The human homologue of
adiponectin (which shares 83% similarity with mouse polypeptide) was originally cloned from adipose tissue and named adipose most abundant gene transcript I (apM-1 ). (3) Finally, a very different approach was employed by Nakano and colleagues (4 l, who
isolated adiponectin from human plasma by virtue of its affinity for gelatin, naming it gelatin-binding protein of 28 KDa (GBP28).
Structure:
Mouse adiponectin is a 30 KDa secreted protein and contains 247 amino acids( 5l,
whereas human adiponectin is a 244 amino acids protein of approximately 28 KDa, which belongs to the complement factor C I q family of proteins. 0 l It contains a 20
residue signal peptide at the amino-terminus; a short non-helical, variable region that show no homology among different species; collagen repeats involved in collagen- triple helix formation; and a globular head at the carboxyl terminus, which shows a very high degree of homology with subunits of C1q and the globular domains of type VIII and type
X collagens(4, S) (Figure: I). (6)
Other data
| Title | STUDY OF PLASMA LEVELS OF ADIPONECTIN AND RESISTIN IN PATIENTS WITH ESSENTIAL HYPERTENSION | Other Titles | دراسة مستوي الاديبونكتين والرزيستين في بلازما مرضي ارتفاع ضغط الدم | Authors | Ahmed Mohamed Moghazy | Issue Date | 2008 |
Attached Files
| File | Size | Format | |
|---|---|---|---|
| Ahmed Mohamed Moghazy.pdf | 1.4 MB | Adobe PDF | View/Open |
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