Heparan Sulfate Affects Elastin Deposition in Fibroblasts Cultured from Donors of Different Ages

2012 ◽  
Vol 15 (1) ◽  
pp. 22-31 ◽  
Author(s):  
Giulia Annovi ◽  
Federica Boraldi ◽  
Pasquale Moscarelli ◽  
Deanna Guerra ◽  
Roberta Tiozzo ◽  
...  
Keyword(s):  
Heparan Sulfate ◽  
Different Ages ◽  
Elastin Deposition

Localization of cell-surface and basement-membrane heparan-sulfate proteoglycans using the malaria circumsporozoite protein

1994 ◽  
Vol 52 ◽  
pp. 294-295
Author(s):  
U. Frevert ◽  
S. Sinnis ◽  
C. Cerami ◽  
V. Nussenzweig
Keyword(s):  
Heparan Sulfate ◽  
Protein A ◽  
Kidney Tissue ◽  
Plasmodium Species ◽  
Its Region ◽  
Basement Membranes ◽  
Heparan Sulfate Proteoglycans ◽  
Infected Mosquito ◽  
Complement Components ◽  
Region Ii

Malaria sporozoites, which invade hepatocytes within minutes after transmission by an infected mosquito, are covered with the circumsporozoite (CS) protein, which in all Plasmodium species contains the conserved region II-plus. This region is also found as a cell-adhesive motif in a variety of host proteins like thrombospondin, properdin and the terminal complement components.The CS protein with its region II-plus specifically binds to heparan sulfate proteoglycans (HSPG) on the basolateral surface of hepatocytes in the space of Disse (FIG. 1), to certain basolateral cell membranes and basement membranes of the kidney (FIG. 2) as well as to heparin in the granules of connective tissue mast cells. The distribution of the HSPG receptors for the CS protein was examined by incubation of Lowicryl K4M or LR White sections of liver and kidney tissue with the recombinant CS ligand, whose binding sites were detected with a monoclonal anti-CS antibody and protein A gold.

Confidence and accuracy of eyewitness memory for target faces at different ages

2013 ◽  
Author(s):  
Christopher D. Kimbrough ◽  
Brian H. Bornstein ◽  
Heather Bryden
Keyword(s):  
Eyewitness Memory ◽  
Different Ages

Specific Cross-reaction of IgG Anti-phospholipid Antibody with Platelet Glycoprotein IIIa

1996 ◽  
Vol 75 (01) ◽  
pp. 168-174 ◽  
Author(s):  
Shigeru Tokita ◽  
Morio Arai ◽  
Naomasa Yamamoto ◽  
Yasuhiro Katagiri ◽  
Kenjiro Tanoue ◽  
...  
Keyword(s):  
Platelet Aggregation ◽  
Heparan Sulfate ◽  
Disulfide Bonds ◽  
Dextran Sulfate ◽  
Human Platelets ◽  
Platelet Glycoprotein ◽  
Activated Platelets ◽  
Fibrinogen Binding ◽  
Dose Dependent Fashion ◽  
Glycoprotein Iiia

SummaryTo study the pathological functions of anti-phospholipid (anti-PL) antibodies, we have analyzed their effect on platelet function. We identified an IgG anti-PL mAb, designated PSG3, which cross-reacted specifically with glycoprotein (GP) IIIa in human platelets and inhibited platelet aggregation. PSG3 bound also to certain polyanionic substances, such as double-stranded DNA, heparan sulfate, dextran sulfate and acetylated-LDL, but not to other polyanionic substances. The binding of PSG3 to GPIIIa was completely inhibited by heparan sulfate and dextran sulfate, indicating that PSG3 recognizes a particular array of negative charges expressed on both GPIIIa and the specified polyanionic substances. Since neither neuraminidase- nor endoglycopeptidase F-treatment of GPIIIa had any significant effect on the binding of PSG3, this array must be located within the amino acid sequence of GPIIIa but not in the carbohydrate moiety. Reduction of the disulfide bonds in GPIIIa greatly reduced its reactivity, suggesting that the negative charges in the epitope are arranged in a particular conformation. PSG3 inhibited platelet aggregation induced by either ADP or collagen, it also inhibited fibrinogen binding to activated platelets in a dose-dependent fashion. PSG3, however, did not inhibit the binding of GRGDSP peptide to activated platelets. These results suggest that the PSG3 epitope on GPIIIa contains a particular array of negative charges, and possibly affects the fibrinogen binding to GPIIb/IIIa complex necessary for platelet aggregation.

Al-Rasm al-ʿUthmānī: Towards Correct Pronunciation and the Preclusion of Ambiguity

2011 ◽  
Vol 13 (2) ◽  
pp. 201-171
Author(s):  
Nāṣir Al-Dīn Abū Khaḍīr
Keyword(s):  
Specific Pattern ◽  
Writing Style ◽  
The Third ◽  
The Past ◽  
Different Ages ◽  
Correct Pronunciation ◽  
The One ◽  
The Mind

The ʿUthmānic way of writing (al-rasm al-ʿUthmānī) is a science that specialises in the writing of Qur'anic words in accordance with a specific ‘pattern’. It follows the writing style of the Companions at the time of the third caliph, ʿUthmān b. ʿAffān, and was attributed to ʿUthmān on the basis that he was the one who ordered the collection and copying of the Qur'an into the actual muṣḥaf. This article aims to expound on the two fundamental functions of al-rasm al-ʿUthmānī: that of paying regard to the ‘correct’ pronunciation of the words in the muṣḥaf, and the pursuit of the preclusion of ambiguity which may arise in the mind of the reader and his auditor. There is a further practical aim for this study: to show the connection between modern orthography and the ʿUthmānic rasm in order that we, nowadays, are thereby able to overcome the problems faced by calligraphers and writers of the past in their different ages and cultures.

Sign in / Sign up

Export Citation Format

Share Document