نتایج جستجو برای: igf binding protein i

تعداد نتایج: 2361947  

Journal: :مجله غدد درون ریز و متابولیسم ایران 0
آزیتا پروانه تفرشی a. parvaneh tafreshi پژوهشگاه ملی مهندسی ژنتیک و زیست فناوری تهران، صندوق پستی 161-14965، دکتر آزیتا پروانه تفرشی راضیه جلال r jalal شمیلا درویش علی پور s darvishalipour حوری سپهری h sepehri خسرو عادلی k adeli

abstract introduction: there is limited knowledge available on the metabolism of glucose in the brain, an insulin insensitive organ. insulin receptors hybridize with insulin like growth factor receptor (igf-i) to transduce the signals in different areas of the brain. in this article we aimed at investigating whether the expression of igf-i receptor and igf-i binding proteins (igfbp1) is changed...

جلال, راضیه, درویش علی پور, شمیلا, سپهری, حوری, عادلی, خسرو, پروانه تفرشی, آزیتا,

Abstract Introduction: There is limited knowledge available on the metabolism of glucose in the brain, an insulin insensitive organ. Insulin receptors hybridize with insulin like growth factor receptor (IGF-I) to transduce the signals in different areas of the brain. In this article we aimed at investigating whether the expression of IGF-I receptor and IGF-I binding proteins (IGFBP1) is change...

اشتیاقی, رادینا, حلاج زاده, جمال , خسروبیگی, علی , دایر, دیان , ضرغامی, نصرت الله ,

Diabetes is a common endocrine disease with complications such as retinopathy, nephropathy and neuropathy which has its monitoring through biomarkers desirable. At present, glycosylated hemoglobin (HbAic) is used for monitoring the long term control of glucose levels in diabetic patients. However, absence of a standardized range, has led to investigations that recently have suggested insulin-li...

Journal: :acta medica iranica 0
m. razzaghy-azar m. nourbakhsh f. hajighasemi

primary growth hormone insensitivity syndrome (ghis) is a rare entity which can be due to defects in growth hormone (gh) receptor that is called type 1 laron syndrome (t1ls) or post receptor defects (type 2 laron syndrome ). the aim of study was determining the clinical and hormonal milieu of the patients with primary ghis and their response to igf-i (insulin like growth factor-i) generation te...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1987
R G Elgin W H Busby D R Clemmons

The insulin-like growth factors IGF-I and IGF-II circulate in blood bound to carrier proteins. The higher molecular mass IGF-binding protein complex (150 kDa) is composed of subunits, and one subunit that forms this complex is growth hormone dependent. In addition, many cell types and tissues secrete another form of IGF binding protein that is not growth hormone dependent. Both forms of the IGF...

Journal: :The Journal of biological chemistry 1990
D R Clemmons M A Cascieri C Camacho-Hubner R H McCusker M L Bayne

Insulin-like growth factor (IGF)-binding proteins (BPs) bind IGF-I and IGF-II with high affinity. They are present in extracellular fluids and modulate the interactions of their ligands with the type 1 IGF cell surface receptor. These studies utilized IGF-I analogs that have reduced binding affinity for either the type 1 IGF receptor or binding proteins to study the ligand specificity of IGF-BP...

Journal: :American journal of physiology. Endocrinology and metabolism 2003
Mary Boes Brian L Dake Barbara A Booth Alexander Sandra Mathew Bateman Kevin L Knudtson Robert S Bar

Specific binding of IGF-binding protein (IGFBP)-3 was shown to be present in the isolated, beating rat heart. The uptake of perfused (125)I-labeled IGF-I in the beating heart was decreased to 9% by blocking IGF-I binding sites with the IGF-I analog Long R(3) (LR(3)) IGF-I. When LR(3) was perfused with complexes of (125)I-IGF-I. IGFBP-3, uptake of (125)I-IGF-I was decreased to 41%, which was sig...

Journal: :The Journal of biological chemistry 1986
C Mottola R G MacDonald J L Brackett J E Mole J K Anderson M P Czech

A protein preparation that specifically binds insulin-like growth factors (IGFs) I and II was purified from medium conditioned by rat liver BRL-3A cells using molecular sieve chromatography in 1 M acetic acid followed by affinity chromatography on IGF-II-agarose. The affinity-purified IGF-binding protein exhibits a single major band with apparent Mr = 36,300 under reducing conditions on sodium ...

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