Use of the weighted jackknife method to calculate the variance in cellular-specific protein secretion rate: Application to monoclonal antibody secretion rate kinetics in response to osmotic stress

1996 ◽  
Vol 50 (2) ◽  
pp. 184-196 ◽  
Author(s):  
Xianhui Yang ◽  
Gary W. Oehlert ◽  
Michael C. Flickinger
Keyword(s):  
Monoclonal Antibody ◽  
Osmotic Stress ◽  
Protein Secretion ◽  
Specific Protein ◽  
Secretion Rate ◽  
Jackknife Method ◽  
Rate Kinetics ◽  
Antibody Secretion

Expression of Platelet Membrane Glycoprotein V in Human Megakaryocytes and Megakaryocytic Cell Lines: A Study Using a Novel Monoclonal Antibody against GPV

1994 ◽  
Vol 72 (05) ◽  
pp. 762-769 ◽  
Author(s):  
Toshiro Takafuta ◽  
Kingo Fujirmura ◽  
Hironori Kawano ◽  
Masaaki Noda ◽  
Tetsuro Fujimoto ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Cell Lines ◽  
Immunohistochemical Analysis ◽  
Specific Protein ◽  
Platelet Membrane ◽  
Rt Pcr ◽  
Chain Reaction ◽  
Flow Cytometric ◽  
Polymerase Chain ◽  
Megakaryocytic Cell

SummaryGlycoprotein V (GPV) is a platelet membrane protein with a molecular weight of 82 kD, and one of the leucine rich glycoproteins (LRG). By reverse transcription-polymerase chain reaction (RT-PCR), GPV cDNA was amplified from mRNA of platelets and megakaryocytic cell lines. However, since there are few reports indicating whether GPV protein is expressed in megakaryocytes as a lineage and maturation specific protein, we studied the GPV expression at the protein level by using a novel monoclonal antibody (1D9) recognizing GPV. Flow cytometric and immunohistochemical analysis indicated that GPV was detected on the surface and in the cytoplasm of only the megakaryocytes in bone marrow aspirates. In a megakaryocytic cell line UT-7, GPV antigen increased after treatment with phorbol-12-myri-state-13-acetate (PMA). These data indicate that only megakaryocytes specifically express the GPV protein among hematopoietic cells and that the expression of GPV increases with differentiation of the megakaryocyte as GPIb-IX complex.

Reactions of human antibodies with CR1 immobilised by mouse monoclonal antibody E11 Red cell phenotype Murine MAb Human anti- Absorbance Ratio Kn(a+) ] Kn(a-) E11 Kna 0.755 0.195 4:1 McC(a+) 0.538 McC(a-) E11 McC 0.136 4:1 Yk(a+) 0.315 Yk(a-) E11 Yka 0.120 26:1 Sl(a+) 0.342 Sl(a-) E11 Sla 0.074 4.6:1 Cs(a+) 0.139 Cs(a-) E11 Cs 0.108 Mapping relative positions of antigens on a specific protein When several murine monoclonal antibodies to different epitopes on the same protein are available, MAIEA can be used to study the relative position of antigens on that protein. This application of MAIEA depends on mutual inhibition of murine monoclonal antibodies and human antibodies. A negative result is obtained when human and monoclonal antibodies compete for the same epitope, or bind to very closely located epitopes, so no tri-molecular complex is produced. Several monoclonal antibodies to the Kell protein have been used in MAIEA to study the relationships of the Kell system antigens [10]. The decay accelerating factor DAF, CD55, is detected by several monoclonal antibodies. Three antibodies BRIC 230, BRIC 110 and BRIC 216 were known from competitive binding assays to bind to different short consensus repeats (SCR) [11]. So three of the four SCRs of the DAF molecule were positively identified (Table II). Strong positive reactions were observed with all three BRIC antibodies and anti-Cr3, anti-WES8, and anti-WESb showing that MAIEA is a useful techique for studying this system [12]. The results showed that Cr8, WESa, and WESb are not on the first three SCRs and must

1995 ◽  
pp. 190-190
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Molecular Complex ◽  
Specific Protein ◽  
Cell Phenotype ◽  
Binding Assays ◽  
Human Antibodies ◽  
Short Consensus Repeats ◽  
Murine Monoclonal Antibodies ◽  
Competitive Binding Assays

Production and characterization of a monoclonal antibody for sweat-specific protein and its application for sweat identification

2003 ◽  
Vol 117 (2) ◽  
pp. 90-95 ◽  
Author(s):  
Kazunori Sagawa ◽  
Akihiko Kimura ◽  
Yoshifumi Saito ◽  
Hiroshi Inoue ◽  
Seiji Yasuda ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Specific Protein

Induction of Hepatocyte Differentiation by the Extracellular Matrix and an RGD-Containing Synthetic Peptide

1991 ◽  
Vol 252 ◽  
Author(s):  
David J. Mooney ◽  
Robert Langer ◽  
Linda K. Hansen ◽  
Joseph P. Vacanti ◽  
Donald E. Ingber
Keyword(s):  
Extracellular Matrix ◽  
Protein Secretion ◽  
Synthetic Peptide ◽  
Cell Spreading ◽  
Specific Protein ◽  
Hepatocyte Differentiation ◽  
Liver Specific Protein ◽  
Extensive Cell ◽  
Adhesive Interactions

ABSTRACTTo design novel biomaterials for hepatocyte transplantation it will be necessary to determine whether specific extracellular matrix (ECM) molecule(s) or the adhesive interactions between the surface and hepatocytes are responsible for regulation of hepatocyte function. Purified ECM molecules (laminin, fibronectin, types I and IV collagen) and a synthetic peptide containing the arginine-glycine-aspartate (RGD) cell-binding sequence were precoated at defined densities to non-adhesive polystyrene dishes. Hepatocytes cultured on dishes coated with a low density of ECM molecules (1 ng/cm2) maintained a round morphology, and high liver-specific protein secretion rates. In contrast, culturing hepatocytes on increasing ECM densities (50–1000 ng/cm2) resulted in extensive cell spreading, a loss of liver-specific protein secretion, and cell growth. Hepatocytes cultured on dishes coated with the RGD-containing peptide did not spread even on a high density of the peptide (10,000 ng/cm2), and albumin secretion remained high for hepatocytes cultured on all peptide densities (1–10,000 ng/cm2). These results suggest that a variety of ECM molecules and synthetic peptides are capable of inducing hepatocyte differentiation in vitro, and these effects depend on their ability to promote cell spreading.

scholarly journals Immunolocalization of the Smooth Muscle-Specific Protein Calponin in Complex and Mixed Tumors of the Mammary Gland of the Dog: Assessment of the Morphogenetic Role of the Myoepithelium

2002 ◽  
Vol 39 (2) ◽  
pp. 247-256 ◽  
Author(s):  
A. Espinosa de los Monteros ◽  
M. Y. Millán ◽  
J. Ordás ◽  
L. Carrasco ◽  
C. Reymundo ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Smooth Muscle ◽  
Mammary Gland ◽  
Malignant Tumors ◽  
Staining Intensity ◽  
Myoepithelial Cells ◽  
Specific Protein ◽  
Benign Tumors ◽  
Normal Mammary Gland ◽  
Mixed Tumors

The immunohistochemical expression of the smooth muscle-specific protein calponin was studied to assess the contribution of myoepithelial cells to the histogenesis of spindle cells of complex and mixed tumors of the mammary gland of the dog and the origin of cartilage and bone in mixed tumors. Formalin-fixed tissues from 55 benign and malignant tumors (49 also containing surrounding normal mammary gland) were evaluated. Periacinar and periductal myoepithelial cells of all the 49 normal mammary glands were diffusely stained by the anti-human calponin monoclonal antibody. Calponin was found in 53 (98%) of the tumors studied, reacting with the myoepithelium-like cells of 86% of benign tumors and their remnants in 85% of malignant tumors. Five different types of calponin-immunoreactive myoepithelial cells were identified: hypertrophic myoepithelial cells, fusiform cells, stellate myoepithelial cells, rounded (myoepithelial) cells, and chondroblasts. Differences in staining intensity and staining pattern among these five types of cells suggested a transition of myoepithelial cells to chondroblasts. Stromal myofibroblasts also showed calponin immunoreactivity, but they did not react with a cytokeratin 14 monoclonal antibody, which recognizes myoepithelial cells in mammary gland. Calponin appears to be a very sensitive marker of normal and neoplastic myoepithelium in the canine mammary gland, and its identification in different cell types of complex and mixed tumors of the mammary gland of the dog suggests a major histogenetic role for myoepithelial cells.

Impact of Signal Peptides on Furin-2A Mediated Monoclonal Antibody Secretion in CHO Cells

2017 ◽  
Vol 12 (9) ◽  
pp. 1700268 ◽  
Author(s):  
Jian'er Lin ◽  
Shu Hui Neo ◽  
Steven C. L. Ho ◽  
Jessna H. M. Yeo ◽  
Tianhua Wang ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Cho Cells ◽  
Signal Peptides ◽  
Antibody Secretion
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