Sex, age and breed related changes in bovine testosterone and intramuscular collagen

doi:10.1016/0309-1740(84)90021-4

Meat Science

Volume 10, Issue 3, 1984, Pages 187-195

https://doi.org/10.1016/0309-1740(84)90021-4 Get rights and content

Abstract

Longissimus muscle biopsies were obtained from forty bulls and steers representing Charolais, Simmental, Angus and Hereford breeds at 6, 9, 12, 15 and 18 months of age to evaluate the influence of age, breed and sex on the biosynthesis of muscle collagen. Blood samples were collected from each animal at each time period. The blood serum was harvested and assayed for concentrations of testosterone. Total collagen, soluble collagen and insoluble collagen were obtained on each sample. Soluble collagen and testosterone levels were significantly influenced by breed, sex and animal age. Total collagen levels were significantly affected by sex and age. Total collagen and testosterone levels peaked at 12 months of age. Breeds were ranked identically for total collagen and testosterone levels at 12 months. These data indicate that bulls are different from steers in synthesis of intramuscular collagen at or near 12 months of age. The increased synthesis of collagen appears to be influenced by testosterone or some other event associated with puberty. The mechanism of this action remains unclear.

References (23)

R.L. Boccard et al.
Meat Sci.
(1979)
T. Liboriussen et al.
Livest. Prod. Sci.
(1977)
B.B. Andersen et al.
Growth, feed utilization, carcass quality and meat quality in Danish dual-purpose cattle
(1977)
I. Bergman et al.
Anal. Chem.
(1963)
H.R. Cross
H.R. Cross et al.
J. Fd Sci.
(1973)
J.D. Crouse et al.
J. Anim. Sci.
(1983)
B.D. Duncan
Biometrics
(1955)
R.A. Field et al.
J. Anim. Sci.
(1966)
D.E. Goll et al.
J. Fd Sci.
(1964)

D.E. Goll et al.

J. Fd Sci.

(1964)

Cited by (67)

Characteristics of intramuscular collagen in calf-fed Nellore bulls and steers throughout the finishing phase
2023, Meat Science
This study evaluated collagen solubility and gene expression of biomarkers for intramuscular collagen (IMCT) deposition and remodeling in the Longissimus muscle of bulls and steers through the finishing phase. Thirty-six Nellore calves were used (18 bulls and 18 steers), and six of each sexual condition were randomly assigned to be harvested at 0, 100, or 200 days on feed (DOF) to evaluate collagen characteristics in different time points throughout the finishing phase. Bulls showed a greater collagen solubility than steers (P = 0.03). The gene expression of fibrogenic markers (TGFβ1, COL1A1, and COL3A1) and IMCT remodeling mediators (MMPII, TIMPII, and LOX) were not affected by sexual condition or DOF (P > 0.05). Our data indicate that young Nellore bulls have a higher percentage of soluble intramuscular collagen, possibly due to higher collagen remodeling associated with a faster growth rate and muscle hypertrophy. Moreover, castration and DOF did not modify mRNA levels of fibrogenic and collagen remodeling markers.
Meta-analysis of the relationship between collagen characteristics and meat tenderness
2022, Meat Science
Meta-analysis methods were used to investigate the effects of collagen content, solubility and pyridinoline cross-link content on Warner-Bratzler shear force (WBSF) and sensory tenderness in major meat species. Data was collected from the literature on pork, beef and lamb and analyzed independently for each species. The beef data was categorized into subgroups according to muscle (loin and other muscle) and age (young, <18 months and old, ≥18 months). The results showed that in beef, collagen content and pyridinoline cross-link content were positively correlated with WBSF and negatively with sensory tenderness, while collagen solubility was negatively correlated with WBSF. The correlation coefficients were greater in other beef muscles than loin. Significant correlations between collagen content and tenderness attributes were observed in old beef animals. However, non-significant relationships and large variations were found in pork and lamb. More studies with various muscles and ages are required for an in-depth understanding of the relationship between collagen characteristics and meat tenderness.
Relationship between meat quality and intramuscular collagen characteristics of muscles from calf-fed, yearling-fed and mature crossbred beef cattle
2021, Meat Science
Citation Excerpt :
For example, intramuscular collagen concentration of the triceps brachii has been shown to decrease from fetus to yearling in the bovine due to an increase in myofibrillar protein relative to collagen, and to remain stable after that (Boccard et al., 1979; Nakano & Thompson, 1980). Cross et al. (1984) found that total collagen in the longissimus muscle of bulls and steers increased until 12 months of age and then decreased to levels observed prior to that age. In the present study, correlations between total collagen and the proportion of myofibrillar protein in the GM showed that total collagen as determined in the Pyr or EC assays decreased as protein increased in the YF GM (r = −0.70 and − 0.67, P = 0.005 and 0.009, respectively), but only the Pyr assay showed a similar correlation with total collagen in the MC GM (r = −0.61, P = 0.0342).
Intramuscular Ehrlich Chromogen (EC) and pyridinoline (Pyr) concentrations in the gluteus medius (GM) and semitendinosus (ST) from crossbred Angus calf- (n = 14) and yearling-fed (n = 14) steer and mature cow (MC, n = 12) carcasses were related to collagen and intramuscular connective tissue (IMCT) thermal stability and peak Warner-Bratzler shear force (WBSF). In both muscles, Pyr density was greater in MC, while EC concentrations were comparable in calf- and yearling-fed steer muscles and lowest in MC muscles. Thermal denaturation temperature and enthalpy of IMCT were highest in both muscles when from MC, although only total collagen was correlated with WBSF in calf fed-yearling fed steer data. Results confirmed that EC concentration contributed to collagen thermal stability in steer muscles, but decreased it in MC muscles, while Pyr was consistently associated with collagen thermal stability.
Cooked color of precooked ground beef patties manufactured with mature bull trimmings
2019, Meat Science
Lean (80%) ground beef was formulated with 0, 25, 50, 75, or 100% mature bull trimmings, formed into patties, cooked to 71 °C in an air-impingement oven, and stored at −20 °C until reheating to 71 °C either in a microwave oven or on a gas-fired chargrill. Instrumental color of raw patties was not (P ≥ .080) affected by levels of bull trim. After initial cooking, internal cooked redness values were not affected (P ≥ .202) by the proportion of bull trim; however, the internal reheated patty redness increased (greater a* values and lesser HA; P ≤ .001) with increasing proportions of bull trimmings. Formulating ground beef with high levels (>50%) of mature, bull trimmings had minimal effects on raw ground beef color, but patties formulated with the highest proportions of bull trimmings appeared undercooked even after cooking twice to 71 °C.
Contribution of collagen and connective tissue to cooked meat toughness; some paradigms reviewed
2018, Meat Science
Citation Excerpt :
However, is this component of muscle really unchangeable? There is certainly evidence to suggest that the content and heat solubility of IMCT in a given muscle can vary with animal growth rate, and is especially influenced by the effects of testosterone (Cross, Schanbacher, & Crouse, 1984; Fishell, Aberle, Judge, & Perry, 1985). The key question is whether these variations influence the IMCT contribution to the toughness of meat cooked at medium to high temperatures, and here the evidence is less clear.
Variations in the quantity and thermal stability of collagen in intramuscular connective tissue (IMCT) play a role in variations in cooked meat tenderness. This review is focussed on sources of variability, especially in the perimysial IMCT, and challenges some of the accepted ideas about its denaturation behaviour, its contribution to cooking shrinkage at high temperatures and the concept of IMCT as an immutable “background toughness”. IMCT dominates the shear strength of raw and lightly cooked muscle, but at cooking temperatures of 70–80° its contribution is smaller than the myofibrillar component. The thermal denaturation temperature of IMCT collagen given by differential scanning calorimetry at fast heating rates is usually in the range of 62–67 °C, but collagen denaturation is a multistep, non-equilibrium process that is highly heating-rate dependent and can occur at 55–60 °C in slow heating regimes, such as slow roasting or sous-vide cooking. Although it is commonly assumed that collagen shrinkage drives shrinkage of meat and greater cooking losses above 65 °C, an examination of currently available information suggested that there is no evidence to support this idea. The amount and thermal stability of IMCT collagen can be varied by factors manipulating growth rate, and a recent model of these effects is discussed. The characteristics of the thermally-stable fraction of IMCT collagen as the most important component influencing the connective tissue contribution to cooked meat toughness and the need for future work investigating mechanisms to degrade or turnover this specific fraction is suggested.
The effects of gender and muscle type on the mRNA levels of the calpain proteolytic system and beef tenderness during post-mortem aging
2016, Livestock Science
Citation Excerpt :
It has been argued that these inconsistent effects of castration and gender on meat tenderness are due to various intrinsic factors, as well as the production systems and the age at slaughter (Field, 1971; Boccard et al., 1979; Purchas et al., 2002). Accordingly, it has been suggested that older animals could produce much tougher meat (Cross et al., 1984; Gheisari et al., 2007) which may be the case with the animals in the present study where bulls were approximately 7 months younger than the steers and more than 11 months younger than the heifers (Table 3). However, it is important to note that commercial abattoirs prefer to slaughter at equivalent weight, which usually means that the slow growing steers and heifers are usually older.
The objective of this study was to determine the effects of gender and muscle type on the mRNA levels of the calpain system and the tenderization of beef meat. The Longissimus thoracis (LT) and the Semimembranosus (SM) were sampled from each bull, steer and heifer after routine slaughter (Six animals per group). The mRNA levels of µ-calpain, m-calpain, calpain-3 and calpastatin were quantified using real-time PCR. Concurrently, tenderness was determined following the Warner–Bratzler Shearforce (WBSF) procedure and rate of tenderization during post-mortem storage was calculated from the WBSF values of 7d and 35d aged steaks. The results show that bulls had significantly lower (P<0.01) WBSF values than heifers which were accompanied by higher (P<0.01) levels of µ-calpain and calpain-3 mRNA but similar levels of calpastatin as compared to heifers. There was a significantly higher (P<0.05) calpastatin expression in steers, as compared to heifers. However, µ-calpain expression was lower (P<0.05) in heifers whose meat was significantly tougher (P<0.05) than that of steers. Steer meat was slightly tougher than that of bulls, while steers had had a tendency to express higher levels of calpastatin but similar µ-calpain and calpain-3 mRNA. The LT had lower (P<0.05) WBSF values than the SM but these muscles tenderised at the same rate, and had similar mRNA levels for all investigated genes. M-calpain mRNA levels were not significantly affected by muscle and gender (P>0.05). Moreover, calpain 3 was negatively correlated to 7d WBSF values (P<0.05). Despite the small sample size, these results suggest that variations in beef tenderness could be modulated through the differential expression of the members of the calpain system, specifically, µ-calpain, calpain 3 and calpastatin.

View all citing articles on Scopus

View full text

Sex, age and breed related changes in bovine testosterone and intramuscular collagen

Abstract

Meat Sci.

Livest. Prod. Sci.

Growth, feed utilization, carcass quality and meat quality in Danish dual-purpose cattle

Anal. Chem.

J. Fd Sci.

J. Anim. Sci.

Biometrics

J. Anim. Sci.

J. Fd Sci.

J. Fd Sci.