scholarly journals The amino acid sequences of the carboxyl termini of human and mouse hepatic lipase influence cell surface association

2003 ◽  
Vol 44 (7) ◽  
pp. 1306-1314 ◽  
Author(s):  
Robert J. Brown ◽  
Joshua R. Schultz ◽  
Kerry W. S. Ko ◽  
John S. Hill ◽  
Tanya A. Ramsamy ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cell Surface ◽  
Hepatic Lipase ◽  
Amino Acid Sequences ◽  
Human And Mouse

scholarly journals Characterization of human and mouse granulocyte-macrophage-colony-stimulating factors derived from Escherichia coli

1987 ◽  
Vol 247 (1) ◽  
pp. 195-199 ◽  
Author(s):  
J L Schrimsher ◽  
K Rose ◽  
M G Simona ◽  
P Wingfield
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequences ◽  
Natural Material ◽  
Animal Cells ◽  
Colony Stimulating Factors ◽  
E Coli ◽  
Macrophage Colony ◽  
The One ◽  
Human And Mouse

Human and mouse granulocyte-macrophage-colony-stimulating factors (hGM-CSF and mGM-CSF, respectively), isolated from Escherichia coli cells expressing the corresponding human and mouse genes, have been characterized. The observed properties of the proteins have been compared with those properties which can be deduced from the DNA sequence alone and the published properties of natural GM-CSFs. The purified E. coli-derived proteins were found to have the expected molecular masses, amino acid compositions and N- and C-terminal amino acid sequences. The finding of 70-90% unprocessed N-terminal methionine for both proteins is discussed. The four Cys residues were found to be involved in two intramolecular disulphide bonds, linking the first and third, and second and fourth Cys residues. This disulphide bond arrangement is probably the one existing in natural material, since, although not glycosylated, both E. coli-derived proteins showed biological activity (colony stimulating assay for hGM-CSF, and cell proliferation assay for mGM-CSF) comparable with that reported for the respective proteins purified from animal cells.

scholarly journals Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs.

1986 ◽  
Vol 83 (20) ◽  
pp. 7721-7725 ◽  
Author(s):  
S. J. Chan ◽  
B. San Segundo ◽  
M. B. McCormick ◽  
D. F. Steiner
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Human And Mouse

scholarly journals Accumulation of membrane glycoproteins in lysosomes requires a tyrosine residue at a particular position in the cytoplasmic tail.

1990 ◽  
Vol 111 (3) ◽  
pp. 955-966 ◽  
Author(s):  
M A Williams ◽  
M Fukuda
Keyword(s):  
Amino Acid ◽  
Cell Surface ◽  
Chimeric Protein ◽  
Cytoplasmic Tail ◽  
Amino Acid Sequences ◽  
Lysosomal Membrane ◽  
Cdna Clones ◽  
Tyrosine Residue ◽  
Wild Type ◽  
Membrane Glycoproteins

Human lysosome membrane glycoprotein h-lamp-1 is a highly N-glycosylated protein found predominantly in lysosomes, with low levels present at the cell surface. The signal required for delivery of h-lamp-1 to lysosomes was investigated by analyzing the intracellular distribution of h-lamp-1 with altered amino acid sequences expressed from mutated cDNA clones. A cytoplasmic tail tyrosine residue found conserved in chicken, rodent, and human deduced amino acid sequences was discovered to be necessary for efficient lysosomal transport of h-lamp-1 in COS-1 cells. In addition, the position of the tyrosine residue relative to the membrane and carboxyl terminus also determined lysosomal expression. Supplanting the wild-type h-lamp-1 cytoplasmic tail onto a cell surface reporter glycoprotein was sufficient to cause redistribution of the chimera to lysosomes. A similar chimeric protein replacing the cytoplasmic tyrosine residue with an alanine was not expressed in lysosomes. Altered proteins that were not transported to lysosomes were found to accumulate at the cell surface, and unlike wild-type lysosomal membrane glycoproteins, were unable to undergo endocytosis. These data indicate that lysosomal membrane glycoproteins are sorted to lysosomes by a cytoplasmic signal containing tyrosine in a specific position, and the sorting signal may be recognized both in the trans-Golgi network and at the cell surface.

Proteins on the surface of the malaria parasite and cell invasion

Parasitology ◽  
1994 ◽  
Vol 108 (S1) ◽  
pp. S5-S18 ◽  
Author(s):  
A. A. Holder
Keyword(s):  
Amino Acid ◽  
Cell Surface ◽  
Malaria Parasite ◽  
Surface Protein ◽  
Cell Types ◽  
Merozoite Surface Protein ◽  
Amino Acid Sequences ◽  
Specific Cell ◽  
Binding Studies ◽  
Erythrocyte Invasion

SUMMARYThe malaria parasite exists in an extracellular form at several stages in its life cycle. Within the vertebrate host, sporozoites and merozoites have to invade specific cell types. Proteins on the surface of the parasite or externalized from specialized organelles have been implicated as ligands for receptors on the host cell surface. Direct binding studies have identified parasite proteins that interact with the target cell surface. Examination of the deduced amino acid sequences has allowed the identification of primary structural motifs which may have roles in this process. On the sporozoite, the circum-sporozoite protein and sporozoite surface protein-2, a protein initially located within micronemes, have been found to contain an amino acid sequence thought to be involved in mediating recognition of sulphated polysaccharides on the surface of a liver cell. On the merozoite, merozoite surface protein-1 may be involved in the initial recognition of red blood cells; this protein undergoes a complex series of modifications in the time between its synthesis as a precursor molecule and successful erythrocyte invasion. Other merozoite proteins located at the apical end of the parasite have been identified as erythrocyte or reticulocyte binding proteins.

scholarly journals Cell Surface Expression of Biologically Active Influenza C Virus HEF Glycoprotein Expressed from cDNA

1999 ◽  
Vol 73 (10) ◽  
pp. 8808-8812 ◽  
Author(s):  
Andrew Pekosz ◽  
Robert A. Lamb
Keyword(s):  
Amino Acid ◽  
Cell Surface ◽  
Membrane Fusion ◽  
Cytoplasmic Tail ◽  
Surface Expression ◽  
Amino Acid Sequences ◽  
Biologically Active ◽  
Cell Surface Expression ◽  
Dependent Manner ◽  
Influenza C Virus

ABSTRACT The hemagglutinin, esterase, and fusion (HEF) glycoprotein of influenza C virus possesses receptor binding, receptor destroying, and membrane fusion activities. The HEF cDNAs from influenza C/Ann Arbor/1/50 (HEF-AA) and influenza C/Taylor/1223/47 (HEF-Tay) viruses were cloned and expressed, and transport of HEF to the cell surface was monitored by susceptibility to cleavage by exogenous trypsin, indirect immunofluorescence microscopy, and flow cytometry. Previously it has been found in studies with the C/Johannesburg/1/66 strain of influenza C virus (HEF-JHB) that transport of HEF to the cell surface is severely inhibited, and it is thought that the short cytoplasmic tail, Arg-Thr-Lys, is involved in blocking HEF cell surface expression (F. Oeffner, H.-D. Klenk, and G. Herrler, J. Gen. Virol. 80:363–369, 1999). As the cytoplasmic tail amino acid sequences of HEF-AA and HEF-Tay are identical to that of HEF-JHB, the data indicate that cell surface expression of HEF-AA and HEF-Tay is not inhibited by this amino acid sequence. Furthermore, the abundant cell surface transport of HEF-AA and HEF-Tay indicates that their cell surface expression does not require coexpression of another viral protein. The HEF-AA and HEF-Tay HEF glycoproteins bound human erythrocytes, promoted membrane fusion in a low-pH and trypsin-dependent manner, and displayed esterase activity, indicating that the HEF glycoprotein alone mediates all three known functions at the cell surface.

scholarly journals tANCHOR: a novel mammalian cell surface peptide display system

BioTechniques ◽  
2020 ◽  
Author(s):  
Daniel Ivanusic ◽  
Kazimierz Madela ◽  
Heidi Burghard ◽  
Gudrun Holland ◽  
Michael Laue ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cell Surface ◽  
Amino Acid Sequences ◽  
Display System ◽  
Extracellular Loop ◽  
Binding Studies ◽  
Small Proteins ◽  
Potential Applications ◽  
Large Extracellular Loop ◽  
Peptide Display

A novel tool for the presentation of peptides and small proteins on the surface of human cells has been developed. Our tANCHOR system utilizes tetraspanin anchors containing heterologous amino acid sequences inserted instead of the large extracellular loop. This technology allows a highly effective extracellular display of epitopes for antibody binding studies and many other potential applications.

The emergence of man: information from protein systems

1981 ◽  
Vol 292 (1057) ◽  
pp. 121-131 ◽  
Keyword(s):  
Gene Expression ◽  
Amino Acid ◽  
Cell Surface ◽  
Genetic Material ◽  
Amino Acid Sequences ◽  
Tissue Structure ◽  
Protein Amino Acid ◽  
Whole Process ◽  
Definition Of ◽  
Subsequent Selection

Protein amino acid sequences are not directly very informative about the emergence of man from his immediate primate ancestry. But this could be because too little attention has been given to protein systems most relevant to the progress of hominization, those that, through their cell-surface action or enzymatic control of biosynthesis of other key proteins or hormones, can modulate the course of cell and tissue development, and so determine changes in tooth architecture, bone and tissue structure, brain and nerve cell development, etc. There are also the histones and other proteins associated with DNA in the genetic material, which have some modulating influence on gene expression. The whole process of carrying information from the genetic material to a species-reproducible morphology is through a cascade of multiple interlocking systems involving proteins at every turn. It is through changes in balance within these systems, and subsequent selection pressures, that the modulations of primate morphology and behaviour that constitute hominization have proceeded, and the process must be understood in terms of cytobiochemistry to give a fully detailed definition of the evolving human genome.

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