Hastings Kamuzu Banda

Banda, Paul Chiudza

doi:10.1057/9781137478122.0003

Cited by 6 publications

(5 citation statements)

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“…. am round to be insensitive to treatment with elastase from human neutrophils [4], but is cleaved by proteases from Staphylococcus aureus [q and elastase from Psrudontotzas aeruginosu [ l8] and macrophages [6]. If the inactivation peptide in human bile is generated by its natural target protease, elastase, this would have a greater possibility to cleave within the exposed region of ol,-antitrypsin in vivo than previously detected in vitro.…”

Section: 2mentioning

confidence: 99%

Identification of hydrophobic fragments of α₁‐antitrypsin and Cl protease inhibitor in human bile, plasma and spleen

et al. 1992

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Hydrophobic peptides were isolated from the phospholipid fraction of human bile, plasma and spleen by exclusion chromatography in organic solvents. From plasma, the activation peptide or Cl protease inhibitor was recovered, from spleen the activation peptide of α1‐antitrypsin, and from bile, both these peptides, as well as a fragment generated by proteolytic cleavage of α1‐antitrypsin six residues N‐terminal of the Pl–Pl ' peptide bond. Cleavages in this region inactivate antiproteases but have previously not been reported to occur in vivo. These peptides in human bile may reflect physiological actions in regulation of antiproteolytic activity or bile secretion processes, and/or be of importance for the physicochemical state of cholesterol, phospholipids and bile acids in bile.

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Section: 2mentioning

confidence: 99%

Identification of hydrophobic fragments of α₁‐antitrypsin and Cl protease inhibitor in human bile, plasma and spleen

et al. 1992

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“…16 The main trigger of disease requires two events: binding of IgG to the cartilage and efficient complement fixation via the alternative and the lectin pathways. 17,18 Complement plays an important role in the initiation and evolution of both RA 19 and osteoarthritis (OA). 20 Downstream complement cleavage products C3a and C5a trigger chemotaxis and activation of neutrophils and monocytes, whereas membrane attack complex C5b-C9 causes cell damage.…”

Section: Introductionmentioning

confidence: 99%

Evaluation of Targeting Efficiency of Joints with Anticollagen II Antibodies

Lofchy¹,

Banda

et al. 2019

Mol. Pharmaceutics

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Diseases of the joints affect over 10% of the world's population, resulting in significant morbidity. There is an unmet need in strategies for specific delivery of therapeutics to the joints. Collagen type II is synthesized by chondrocytes and is mainly restricted to the cartilage and tendons. Arthrogen-CIA is a commercially available anti-collagen II antibody cocktail that reacts with 5 different epitopes on human, bovine, and mouse collagen II. Arthrogen has been used for induction of experimental rheumatoid arthritis (RA) in mice because of high complement activation on the cartilage surface. Native collagen II might serve as a useful target for potential delivery of therapeutics to the joint. To evaluate the efficiency and specificity of targeting collagen II, Arthrogen was labeled with near-infrared (NIR) dye IRDye 800 or IRDye 680. Using ex vivo

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“…For example, proteolytically processed 01,-AT can act as a neutrophil chemoattractant [23], and the infiltrated neutrophils may enhance tissue destruction in the tumor microenvironment.…”

Section: Discussionmentioning

confidence: 99%

Properties of α₁‐antitrypsin secreted by human adenocarcinoma cell lines

et al. 1993

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~,-Antit~psin; (a,-AT) produced by various human carcinoma (non-hepatoma) cell lines were analyzed. Ftve out of eight ceil lines secreted detectable amounts of a,-AT into the ~onditloned media. All were aden~arcinoma cell lines. The tumor cell-derived a,-ATs had higher molecular weights (MW) than the normal plasma form. Most of this difference was an overall reflection of altered ~-~ycosylation. As judged by binding of iectins, the glycosyiation had shifted towards higher levels of triantennary oligosaccharides and higher levels of fucosylation. The condittoned media also contained lower MW

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Hastings Kamuzu Banda

Cited by 6 publications

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Identification of hydrophobic fragments of α₁‐antitrypsin and Cl protease inhibitor in human bile, plasma and spleen

Identification of hydrophobic fragments of α₁‐antitrypsin and Cl protease inhibitor in human bile, plasma and spleen

Evaluation of Targeting Efficiency of Joints with Anticollagen II Antibodies

Properties of α₁‐antitrypsin secreted by human adenocarcinoma cell lines

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Hastings Kamuzu Banda

Cited by 6 publications

References 0 publications

Identification of hydrophobic fragments of α1‐antitrypsin and Cl protease inhibitor in human bile, plasma and spleen

Identification of hydrophobic fragments of α1‐antitrypsin and Cl protease inhibitor in human bile, plasma and spleen

Evaluation of Targeting Efficiency of Joints with Anticollagen II Antibodies

Properties of α1‐antitrypsin secreted by human adenocarcinoma cell lines

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Identification of hydrophobic fragments of α₁‐antitrypsin and Cl protease inhibitor in human bile, plasma and spleen

Identification of hydrophobic fragments of α₁‐antitrypsin and Cl protease inhibitor in human bile, plasma and spleen

Properties of α₁‐antitrypsin secreted by human adenocarcinoma cell lines