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1.
Int J Biometeorol ; 59(6): 733-43, 2015 Jun.
Article in English | MEDLINE | ID: mdl-25172085

ABSTRACT

Seasonal variations in hair length, tick loads, cortisol levels, haematological parameters (HP) and temperature humidity index (THI) in Nguni cows of different colours raised in two low-input farms, and a commercial stud was determined. The sites were chosen based on their production systems, climatic characteristics and geographical locations. Zazulwana and Komga are low-input, humid-coastal areas, while Honeydale is a high-input, dry-inland Nguni stud farm. A total of 103 cows, grouped according to parity, location and coat colour, were used in the study. The effects of location, coat colour, hair length and season were used to determine tick loads on different body parts, cortisol levels and HP in blood from Nguni cows. Highest tick loads were recorded under the tail and the lowest on the head of each of the animals (P < 0.05). Zazulwana cows recorded the highest tick loads under the tails of all the cows used in the study from the three farms (P < 0.05). High tick loads were recorded for cows with long hairs. Hair lengths were longest during the winter season in the coastal areas of Zazulwana and Honeydale (P < 0.05). White and brown-white patched cows had significantly longer (P < 0.05) hair strands than those having a combination of red, black and white colour. Cortisol and THI were significantly lower (P < 0.05) in summer season. Red blood cells, haematoglobin, haematocrit, mean cell volumes, white blood cells, neutrophils, lymphocytes, eosinophils and basophils were significantly different (P < 0.05) as some associated with age across all seasons and correlated to THI. It was concluded that the location, coat colour and season had effects on hair length, cortisol levels, THI, HP and tick loads on different body parts and heat stress in Nguni cows.


Subject(s)
Cattle/physiology , Cattle/parasitology , Hair/physiology , Hydrocortisone/blood , Seasons , Ticks , Africa , Agriculture/statistics & numerical data , Animals , Female , Hair/parasitology , Heat-Shock Response , Humidity , Parasite Load , Temperature
2.
Asian-Australas J Anim Sci ; 27(11): 1663-70, 2014 Nov.
Article in English | MEDLINE | ID: mdl-25358328

ABSTRACT

The objective of this study was to determine the perceptions and knowledge of farmers of heat stress and tick resistance in cattle. A cross-sectional survey was conducted and 110 farmers in four villages in the sour and sweet velds of the Eastern Cape Province, South Africa were interviewed. The associations among area (municipality), gender, age, level of education, employment and religion were computed using Chi-square tests. The majority of the respondents had on average 4 bulls, 4 cows, 4 heifers, 4 calves, and 4 oxen. Milk was considered as the major (28.3%) reason for keeping cattle. Most farmers owned non-descript (72.6%), and Nguni (45.3%) cattle because of their heat tolerance (54.7%), tick resistance (54.7%), and milking ability (28.2%) traits. Excessive panting (56.6%) and disease transmission (76%) were regarded as the major effects of heat stress and tick infestation in cattle, respectively. About 50% of the respondents agreed that hair length influences tick resistance and 47.17% considered coat colour when acquiring cattle. In the sampled areas, ticks were prevalent in the summer season (93%), and 77.36% of the respondents use acaricides every fortnight. Gall sickness was reported to be a major problem in the cattle herds by 36.79% of the respondents. Our results showed that farmers in the two municipalities had knowledge of cattle adaptation to heat stress and tick resistance.

3.
J Thromb Haemost ; 2(12): 2170-7, 2004 Dec.
Article in English | MEDLINE | ID: mdl-15613023

ABSTRACT

It is now apparent that the inactivated latent and cleaved conformers of antithrombin (AT) are of pathological significance. Using a single-run electrophoretic technique that allows the quantitative assessment of these conformers in 2 microL plasma, we show that near 3% of the total AT in the circulations of normal individuals is in latent conformation. Only trace amounts of cleaved AT were observed. The slow decline in AT activity on incubation of plasma at 37 degrees C was shown to be almost wholly due to a transition of native AT to its inactive latent form. Also initial studies in the rabbit indicate that the latent form, like the cleaved, has an identical circulatory half-life to that of native AT. We deduce that the steady concentration of latent AT in the circulation is due to the transition of some 10(12) molecules of AT per second balanced by an equivalent clearance of the latent form. Examples of clinical applications of the new technique include its use as a comprehensive single-step screen for genetic variants associated with AT deficiency, and notably the potential it provides to monitor the changes responsible for the loss of AT in the shock syndromes.


Subject(s)
Antithrombins/analysis , Antithrombins/chemistry , Blood Circulation , Electrophoresis, Polyacrylamide Gel/methods , Animals , Cattle , Factor Xa/chemistry , Humans , Models, Molecular , Protein Conformation , Protein Denaturation , Protein Folding , Protein Structure, Secondary , Rabbits , Serpins/chemistry , Temperature , Time Factors , Urea/pharmacology
4.
J Thromb Haemost ; 2(6): 931-9, 2004 Jun.
Article in English | MEDLINE | ID: mdl-15140129

ABSTRACT

BACKGROUND: Missense mutations causing conformational alterations in serpins can be responsible for protein deficiency associated with human diseases. However, there are few data about conformational consequences of mutations affecting antithrombin, the main hemostatic serpin. OBJECTIVES: To investigate the conformational and clinical effect of mutations affecting the shutter region of antithrombin. PATIENTS AND METHODS: We identified two families with significant reduction of circulating antithrombin displaying early and severe venous thrombosis, frequently associated with pregnancy or infection. Mutations were determined by standard molecular methods. Biochemical studies were performed on plasma samples. One variant (P80S) was purified by heparin-affinity chromatography and gel filtration, and evaluated by proteomic analysis. Finally, we modelled the structure of the mutant dimer. RESULTS: We identified two missense mutations affecting the shutter region of antithrombin: P80S and G424R. Carriers of both mutations presented traces of a similar abnormal antithrombin, supporting inefficiently expressed rather than non-expressed variants. The abnormal antithrombin purified from P80S carriers is an inactive disulfide-linked dimer of mutant antithrombin whose properties are consistent with head-to-head insertion of the reactive loop. CONCLUSIONS: Our data support the conclusion that missense mutations affecting the shutter region of serpins have specific conformational effects resulting in the formation of mutant oligomers. The consequent inefficiency of secretion explains the accompanying deficiency and loss of function, but the severity of thrombosis associated with these mutations suggests that the oligomers also have new and undefined pathological properties that could be exacerbated by pregnancy or infection.


Subject(s)
Antithrombin III Deficiency/genetics , Antithrombin III/genetics , Disulfides , Mutation, Missense , Venous Thrombosis/genetics , Adult , Aged , Antithrombin III/chemistry , Antithrombin III/isolation & purification , Antithrombin III Deficiency/complications , DNA Mutational Analysis , Dimerization , Family Health , Female , Humans , Male , Middle Aged , Pedigree , Protein Conformation , Serpins/chemistry , Serpins/genetics , Spain , Venous Thrombosis/blood
5.
Thromb Haemost ; 86(1): 14-22, 2001 Jul.
Article in English | MEDLINE | ID: mdl-11487000

ABSTRACT

Antithrombin readily undergoes a spontaneous transition from its active five-stranded form to a six-stranded inactive latent form. The recognition of this change in plasma has been obscured by the immediate linkage of newly formed latent antithrombin to a molecule of active antithrombin to give a dimer with an electrophoretic mobility readily confused with that of native active antithrombin. A new micromethod now allows unequivocal identification of latent antithrombin in whole plasma. This shows that at 37 degrees C some 10% of plasma antithrombin is converted to the latent form in 24 h. The rate of conversion is greatly accelerated at increased temperatures, as occurs in the pasteurisation of plasma concentrates that should now be checked for efficacy. But increased transition also occurs in the plasma at the slightly increased temperatures that accompany incidental infections. This is of particular significance if there is a conformationally unstable variant of antithrombin; here fever can provoke a sudden transition with the onset of a characteristically severe episode of thromboembolism. Such variants are not rare and include those previously classified as pleiotropic. The precise structural pathway, now known with antithrombin, provides a model of the changes occurring in other conformational diseases, including Alzheimer's and the prion dementias.


Subject(s)
Antithrombins/chemistry , Thrombosis/etiology , Antithrombins/analysis , Antithrombins/genetics , Fever/complications , Genetic Variation , Humans , Protein Conformation , Serpins/chemistry , Temperature
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