Prevention of Attachment of Phosphorylcholine to a Major Excretory-Secretory Product of Acanthocheilonema viteae Using Tunicamycin

1996 ◽  
Vol 82 (2) ◽  
pp. 320 ◽  
Author(s):  
Katrina M. Houston ◽  
William Harnett
Keyword(s):  
Secretory Product ◽  
Acanthocheilonema Viteae

Association between circulating antigen and parasite load in a model filarial system, Acanthocheilonema viteae in jirds

Parasitology ◽  
1990 ◽  
Vol 101 (3) ◽  
pp. 435-444 ◽  
Author(s):  
W. Harnett ◽  
M. J. Worms ◽  
M. Grainger ◽  
S. D. M. Pyke ◽  
R. M. E. Parkhouse
Keyword(s):  
Significant Relationship ◽  
Worm Burden ◽  
Parasite Burden ◽  
Parasite Load ◽  
Secretory Product ◽  
Antigen Level ◽  
Blood Samples ◽  
Acanthocheilonema Viteae ◽  
Circulating Antigen ◽  
Detectable Antigen

SUMMARYJirds (Meriones libycus) were infected with various numbers of Acanthocheilonema viteae L3 stage parasites. During the course of the ensuing 16 weeks, blood samples were collected at 2 weekly intervals and the amount of the major parasite excretory–secretory product (E–S 62) and antibodies directed against it measured. After 16 weeks, animals were sacrificed and the size of the mature worm burden established. In spite of interaction between E–S 62 and host antibody, a statistically significant relationship was found to exist between the amount of E–S 62 present in the bloodstream and the size of the parasite load. It is suggested that the detectable antigen level is more influenced by the size of the worm burden than the presence of antibody and that antibody is only likely to affect adversely antigen measurement in situations where the amount released is relatively low. Examples of this are early in infection and in low-level infections. These ideas are discussed in relation to the development and assessment of serological assays which attempt to predict parasite burden in human filarial infections.

Origin, kinetics of circulation and fate in vivo of the major excretory–secretory product of Acanthocheilonema viteae

Parasitology ◽  
1989 ◽  
Vol 99 (2) ◽  
pp. 229-239 ◽  
Author(s):  
W. Harnett ◽  
M. J. Worms ◽  
A. Kapil ◽  
M. Grainger ◽  
R. M. E. Parkhouse
Keyword(s):  
Molecular Weight ◽  
Life Cycle ◽  
Half Life ◽  
Secretory Product ◽  
Parasite Life Cycle ◽  
Acanthocheilonema Viteae ◽  
Sds Page ◽  
Kinetics Of ◽  
Immunohistological Analysis

SummaryThe excretions-secretions (E-S) of Acanthocheilonema viteae consist mainly of one product, molecular weight 62 kDa. This molecule is synthesized during the vertebrate phase of the parasite life-cycle and is first detectable in the E-S of L4 parasites. It is cross-reactive with E-S of human filarial parasites as a consequence of possessing a phosphorylcholine (PC) moiety. The 62 kDa molecule has been employed as a model for the study of the origin and fate of filarial E-S. Immunohistological analysis has shown the molecule to be located predominantly in the parasite gut. Transplantation of adult female [S] methionine pulsed worms into uninfected jirds resulted in the radio-labelled secreted 62 kDa antigen being detected in the bloodstream within 4 h by SDS–PAGE/immunoprecipitation analysis. The systemic half-life of the molecule as estimated by clearance of injected, purified I-labelled material was measured in naive and infected jird hosts.

Control of Secretory Production in the Isopod Hepatopancreas

1972 ◽  
Vol 30 ◽  
pp. 166-167
Author(s):  
John W. Roberts ◽  
E. R. Witkus
Keyword(s):  
B Cells ◽  
Morphological Data ◽  
Secretory Product ◽  
Secretory Function ◽  
Secretory Material ◽  
Blind Ending ◽  
Secretory Production ◽  
Regenerative Cells ◽  
Immature Cells ◽  
And Storage

The isopod hepatopancreas, as exemplified by Oniscus ascellus. is comprised of four blind-ending diverticula. The regenerative cells at the tip of each diverticula differentiate into either club-shaped B-cells, which serve a secretory function, or into conoid S-cells, which serve in the absorption and storage of nutrients.The glandular B-cells begin producing secretory material with the development of rough endoplasmic reticulum during their process of maturation from the undifferentiated regenerative cells. Cytochemical and morphological data indicate that the hepatopancreas sequentially produces two types of secretory material within the large club-shaped cells. The production of the carbohydrate-like secretory product in immature cells seems to be phased out as the production of the osmiophilic secretion was phased in as the cell matured.

HISTOMORPHOLOGICAL CHANGES IN THE BRAIN IN RELATION TO OVARIAN CYCLE OF FRESHWATER CRAB, BARYTELPHUSA CUNICULARIS

2017 ◽  
Vol 23 (1) ◽  
Author(s):  
C.A. JAWALE
Keyword(s):  
Staining Intensity ◽  
Neurosecretory Cells ◽  
Ovarian Cycle ◽  
Secretory Product ◽  
Freshwater Crab ◽  
Intensity Index ◽  
Cytoplasmic Material ◽  
Histomorphological Changes ◽  
Cyclic Changes ◽  
The Brain

Ovarian maturation by neurosecretory cells in the brain of freshwater crab, Barytelphusa cunicularis have been examined. The histological scrutiny of the brain of Barytelphusa cunicularis related with three types (A, B and C) of neurosecretory cells, which are classified on the basis of size, shape and tinctorial characters. All these types of cells marked annual cyclic changes of cytoplasmic material in association with ovarian cycle. The activity of these cells has been correlated with the ovarian cycle. They are distinguishable by their size, nature locations, shape, nucleus position, cell measure and the secretory product in the cytoplasm. The result indicates that the neurosecretory A, B and C cells of the brain seen involved in the process of mating ovulation. The neurosecretory materials staining intensity index of these cells is described.

Heparin induces amyloid formation in cultured human isletss

2007 ◽  
Vol 30 (4) ◽  
pp. 92 ◽  
Author(s):  
K Potter ◽  
K Park
Keyword(s):  
Cell Death ◽  
B Cells ◽  
Islet Transplantation ◽  
Islet Cell ◽  
Human Islets ◽  
Fibril Formation ◽  
Amyloid Formation ◽  
Secretory Product ◽  
Islet Amyloid ◽  
Heparin Sulfate

Background: Pancreatic islet transplantation offers improved glycemic control in type 1 diabetic patients above standard insulin therapy, ideally minimizing macro- and microvascular complications of diabetes mellitus. However success is limited thus far, with fewer than 10% of patients retaining insulin independence at two years post-transplantation. In addition to immune rejection, many non-immune factors may promote long-term graft secretory dysfunction and loss of viable graft mass. One such important non-immune factor may be the formation of islet amyloid, a pathologic lesion of the islet in type 2 diabetes that contributes to the progressive loss of b cells in that disease and that has been shown to form rapidly in human islets transplanted into NOD.scid mice. Amyloid deposits are composed primarily of the b cell secretory product islet amyloid polypeptide (IAPP), are cytotoxic, and develop in environments in which b cells are stressed. Heparin sulfate is used as an anti-coagulant in clinical islet transplantation and to prevent the instant blood-mediated inflammatory reaction (IBMIR), which occurs upon contact between islets and blood and may destroy a substantial proportion of the grafted islet mass. However, heparin is also known to stimulate amyloid fibril formation. Methods: To determine whether heparin may enhance amyloid formation in human islets and contribute to graft failure, we cultured isolated human islets in the presence or absence of heparin sulfate (42 and 420 units/ml) for 2 weeks in 11.1 mM glucose. Results: Histological assessment of sections of cultured islets for the presence of amyloid (by thioflavin S staining) revealed a marked, concentration-dependent increase in amyloid deposition following culture in the presence of heparin. Quantitative analysis of these sections showed that the proportion of islet area comprised of amyloid was increased approximately 2-fold (0.15%±0.12% vs 0.46%±0.15% of islet area) following culture in 42 units/ml heparin, and the proportion of islets in which amyloid was detectable (amyloid prevalence) was also increased (35%±24% vs 68%±10% of islets). At 420 units/ml heparin, the amyloid area was even greater (0.23%±0.15% vs 0.97%±0.42% of islet area) as was the amyloid prevalence (53%±29% vs 81%±14% of islets). To affirm that heparin can stimulate IAPP fibrillogenesis and enhance IAPP toxicity, we incubated synthetic human IAPP in the presence of heparin and measured amyloid formation in real time by thioflavin T fluorescence, and cell toxicity by Alamar blue viability assay in transformed rat (INS-1) ß-cell cultures. Heparin stimulated IAPP fibril formation and increased death of INS-1 cells exposed to IAPP (78.2%±10.9% vs 51.8%±12.2% of control viability), suggesting that heparin stimulates IAPP aggregation and toxicity. Remarkably, preliminary assessment of human islets cultured in heparin did not show increased islet cell death by TUNEL staining or loss of insulin immunostaining. Conclusion: In summary, heparin increases amyloid formation in cultured human islets. Although our preliminary data does not suggest that heparin-induced amyloid formation contributes to islet cell death, we speculate that heparin-induced amyloid formation may contribute to graft dysfunction and that caution should be used in the clinical application of this drug in islet transplantation.

A Review on Melatonin’s Effects in Cancer: Potential Mechanisms

2018 ◽  
Vol 18 (7) ◽  
pp. 985-992 ◽  
Author(s):  
Aysegul Hanikoglu ◽  
Ertan Kucuksayan ◽  
Rana Cagla Akduman ◽  
Tomris Ozben
Keyword(s):  
Systematic Review ◽  
Antioxidant Activity ◽  
Membrane Receptors ◽  
Cancer Development ◽  
Secretory Product ◽  
Prevention And Treatment ◽  
G Protein Coupled

This systematic review aims to elucidate the role of melatonin (N-acetyl-5-metoxy-tryptamine) (MLT) in the prevention and treatment of cancer. MLT is a pineal gland secretory product, an evolutionarily highly conserved molecule; it is also an antioxidant and an impressive protector of mitochondrial bioenergetic activity. MLT is characterized by an ample range of activities, modulating the physiology and molecular biology of the cell. Its physiological functions relate principally to the interaction of G Protein-Coupled MT1 and MT2 trans-membrane receptors (GPCRs), a family of guanidine triphosphate binding proteins. MLT has been demonstrated to suppress the growth of various tumours both, in vivo and in vitro. In this review, we analyze in depth, the antioxidant activity of melatonin, aiming to illustrate the cancer treatment potential of the molecule, by limiting or reversing the changes occurring during cancer development and growth.

Metallothionein gene expression and secretion in white adipose tissue

2000 ◽  
Vol 279 (6) ◽  
pp. R2329-R2335 ◽  
Author(s):  
Paul Trayhurn ◽  
Jacqueline S. Duncan ◽  
Anne M. Wood ◽  
John H. Beattie
Keyword(s):  
Gene Expression ◽  
Molecular Weight ◽  
Adipose Tissue ◽  
White Adipose Tissue ◽  
Stromal Vascular Fraction ◽  
Low Molecular Weight ◽  
Secretory Product ◽  
Mrna Levels ◽  
Gene Encoding ◽  
Adrenoceptor Agonist

White adipose tissue (WAT) has been examined to determine whether the gene encoding metallothionein (MT), a low-molecular-weight stress response protein, is expressed in the tissue and whether MT may be a secretory product of adipocytes. The MT-1 gene was expressed in epididymal WAT, with MT-1 mRNA levels being similar in lean and obese ( ob/ ob) mice. MT-1 mRNA was found in each of the main adipose tissue sites (epididymal, perirenal, omental, subcutaneous), and there was no major difference between depots. Separation of adipocytes from the stromal-vascular fraction of WAT indicated that the MT gene (MT-1 and MT-2) was expressed in adipocytes themselves. Treatment of mice with zinc had no effect on MT-1 mRNA levels in WAT, despite strong induction of MT-1 expression in the liver. MT-1 gene expression in WAT was also unaltered by fasting or norepinephrine. However, administration of a β3-adrenoceptor agonist, BRL-35153A, led to a significant increase in MT-1 mRNA. On differentiation of fibroblastic preadipocytes to adipocytes in primary culture, MT was detected in the medium, suggesting that the protein may be secreted from WAT. It is concluded that WAT may be a significant site of MT production; within adipocytes, MT could play an antioxidant role in protecting fatty acids from damage.

Cellular and Chemical Events During Enamel Maturation

1998 ◽  
Vol 9 (2) ◽  
pp. 128-161 ◽  
Author(s):  
C.E. Smith
Keyword(s):  
Crystal Growth ◽  
Driving Forces ◽  
Morphological Changes ◽  
Matrix Proteins ◽  
Secretory Product ◽  
Water Matrix ◽  
Mineralized Tissues ◽  
Progressive Growth ◽  
Chemical Events ◽  
Protein Rich

This review focuses on the process of enamel maturation, a series of events associated with slow, progressive growth in the width and thickness of apatitic crystals. This developmental step causes gradual physical hardening and transformation of soft, newly formed enamel into one of the most durable mineralized tissues produced biologically. Enamel is the secretory product of specialized epithelial cells, the ameloblasts, which make this covering on the crowns of teeth in two steps. First, they roughly "map out" the location and limits (overall thickness) of the entire extracellular layer as a protein-rich, acellular, and avascular matrix filled with thin, ribbon-like crystals of carbonated hydroxyapatite. These initial crystals are organized spatially into rod and interrod territories as they form, and rod crystals are lengthened by Tomes' processes in tandem with appositional movement of ameloblasts away from the dentin surface. Once the full thickness of enamel has been formed, ameloblasts initiate a series of repetitive morphological changes at the enamel surface in which tight junctions and deep membrane infoldings periodically appear (ruffle-ended), then disappear for short intervals (smooth-ended), from the apical ends of the cells. As this happens, the enamel covered by these cells changes rhythmically in net pH from mildly acidic (ruffle-ended) to near-physiologic (smooth-ended) as mineral crystals slowly expand into the "spaces" (volume) formerly occupied by matrix proteins and water. Matrix proteins are processed and degraded by proteinases throughout amelogenesis, but they undergo more rapid destruction once ameloblast modulation begins. Ruffle-ended ameloblasts appear to function primarily as a regulatory and transport epithelium for controlling the movement of calcium and other ions such as bicarbonate into enamel to maintain buffering capacity and driving forces optimized for surface crystal growth. The reason ruffle-ended ameloblasts become smooth-ended periodically is unknown, although this event seems to be crucial for sustaining long-term crystal growth.

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