نتایج جستجو برای: human kallikreins

تعداد نتایج: 1643006  

Journal: :Cancer research 1990
D R Senger D T Connolly L Van de Water J Feder H F Dvorak

Rodent and human tumor cell lines secrete a potent vascular permeability factor (VPF) which causes a rapid and substantial increase in microvascular permeability to plasma proteins without causing mast cell degranulation, or endothelial cell damage or without exciting an inflammatory cell infiltrate [D. R. Senger, S. J. Galli, A. M. Dvorak, C. A. Perruzzi, V. S. Harvey, and H. F. Dvorak. Scienc...

Journal: :Molecular biology of the cell 2007
Celine Deraison Chrystelle Bonnart Frederic Lopez Celine Besson Ross Robinson Arumugam Jayakumar Fredrik Wagberg Maria Brattsand Jean Pierre Hachem Goran Leonardsson Alain Hovnanian

LEKTI is a 15-domain serine proteinase inhibitor whose defective expression underlies the severe autosomal recessive ichthyosiform skin disease, Netherton syndrome. Here, we show that LEKTI is produced as a precursor rapidly cleaved by furin, generating a variety of single or multidomain LEKTI fragments secreted in cultured keratinocytes and in the epidermis. The identity of these biological fr...

Journal: :Clinical biochemistry 2007
Julie L V Shaw Linda Grass Georgia Sotiropoulou Eleftherios P Diamandis

BACKGROUND Human kallikrein 15 (KLK15) may have some utility as a prostate, ovarian, and breast cancer biomarker, based on previous studies, which examined mRNA levels of KLK15. The aim of this study was to develop analytical technology for human kallikrein 15, including recombinant protein, specific antibodies, and a sensitive and specific ELISA immunoassay. The assay was then used to examine ...

Journal: :Clinical chemistry 2003
Carl Kapadia Albert Chang Georgia Sotiropoulou George M Yousef Linda Grass Antoninus Soosaipillai Xuekun Xing David H C Howarth Eleftherios P Diamandis

BACKGROUND The aims of this study were to develop immunologic reagents and a sensitive and specific immunoassay for human kallikrein 13 (hK13) and to examine the presence of hK13 in human tissues and biological fluids. METHODS Recombinant hK13 protein was produced and purified with use of a Pichia pastoris yeast expression system. The protein was used as an immunogen to generate mouse monoclo...

Journal: :Clinical chemistry 2005
Christina V Obiezu Shannon J C Shan Antoninus Soosaipillai Liu-Ying Luo Linda Grass Georgia Sotiropoulou Constantina D Petraki Panos A Papanastasiou Michael A Levesque Eleftherios P Diamandis

BACKGROUND Human kallikrein 4 (hK4) is a proteolytic enzyme belonging to the tissue kallikrein family of serine proteases. Previous tissue expression studies have demonstrated highest KLK4 mRNA expression in prostatic tissue, but there has been only limited evidence for the presence of hK4 protein in prostate and other tissues and in corresponding biological secretions. METHODS To investigate...

پایان نامه :وزارت علوم، تحقیقات و فناوری - دانشگاه علوم و معارف قرآن کریم - دانشکده علوم قرآنی قم 1389

worship is submission and humitility with believe to divinity in fornt of god. in jewish religion ,worship is submission of the god inall the ordes and devosion tohim .worshio is not only so widely in islam and jew and does not include pray and fast and etc but also is every action that human does with divine intention and to content him. worship has huge and excellent rank in qoran and old te...

Journal: :The British journal of dermatology 2007
N Komatsu K Saijoh C Kuk F Shirasaki K Takehara E P Diamandis

BACKGROUND Human tissue kallikreins (KLKs) are a family of 15 trypsin-like or chymotrypsin-like secreted serine proteases (KLK1-KLK15). Multiple KLKs have been quantitatively identified in normal stratum corneum (SC) and sweat as candidate desquamation-related proteases. OBJECTIVES To quantify KLK5, KLK6, KLK7, KLK8, KLK10, KLK11, KLK13 and KLK14 in the SC and serum of patients with psoriasis...

Journal: :The Journal of Experimental Medicine 1986
A Alagon L D Possani J Smart W D Schleuning

We have purified and characterized the major N-benzoyl-L-arginine ethyl ester hydrolase from the venom of Heloderma horridum horridum. The enzyme belongs to the serine proteinase family, and its activity vs. peptide amide substrates and human high-molecular-weight kininogen suggests a similarity to the family of kallikreins. This interpretation is corroborated by its reactivity with the natural...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید