Oral Administration of 14C Labeled Gelatin Hydrolysate Leads to an Accumulation of Radioactivity in Cartilage of Mice (C57/BL)

Abstract

Several investigations showed a positive influence of orally administered gelatin on degenerative diseases of the musculo-skeletal system. Both the therapeutic mechanism and the absorption dynamics, however, remain unclear. Therefore, this study investigated the time course of gelatin hydrolysate absorption and its subsequent distribution in various tissues in mice (C57/BL). Absorption of (14)C labeled gelatin hydrolysate was compared to control mice administered (14)C labeled proline following intragastric application. Plasma and tissue radioactivity was measured over 192 h. Additional "gut sac" experiments were conducted to quantify the MW distribution of the absorbed gelatin using SDS-electrophoresis and HPLC. Ninety-five percent of enterally applied gelatin hydrolysate was absorbed within the first 12 h. The distribution of the labeled gelatin in the various tissues was similar to that of labeled proline with the exception of cartilage, where a pronounced and long-lasting accumulation of gelatin hydrolysate was observed. In cartilage, measured radioactivity was more than twice as high following gelatin administration compared to the control group. The absorption of gelatin hydrolysate in its high molecular form, with peptides of 2.5-15kD, was detected following intestinal passage. These results demonstrate intestinal absorption and cartilage tissue accumulation of gelatin hydrolysate and suggest a potential mechanism for previously observed clinical benefits of orally administered gelatin.

Development and characterization of orally-disintegrating films for propolis delivery

“…Although the capacity of hydrolyzed collagen to form a polymeric matrix has not been proven, it presents other properties, such as assisting bone maintenance because it increases osteoblast activity (GUILLERMINET et al, 2010). Furthermore, hydrolyzed collagen, which is derived from the enzymatic hydrolysis of collagen and not only from acid or alkaline hydrolysis such as gelatin (HOQUE; BENJAKUL; PRODPRAN, 2011), has smaller peptides (OESSER; ADAM; BABEL, 1999), and thus it has higher solubility and possibly affects the characteristics of the film, as well as the process of delivering the active component.…”

Caracterização químico-nutricional de um isolado protéico de soro de leite, um hidrolisado de colágeno bovino e misturas dos dois produtos

“…Sua composição aminoacídica é bastante atípica sendo deficiente em todos os aminoácidos considerados nutricionalmente essenciais com o agravante de não apresentar o triptofano em sua composição 10 , dessa forma, o seu valor nutritivo, com base no escore de aminoácidos essenciais (EAE), poderá ser considerado zero. Por outro lado, várias pesquisas [11][12][13] têm mostrado a importância do colágeno e seus derivados na manutenção e reconstituição da pele, dos ossos, dos tecidos cartilaginosos e da matriz extracelular.…”

“…Embora o perfil aminoacídico do HCB seja incapaz de promover crescimento e manter o balanço de nitrogênio, como única fonte de proteína, foi o melhor substrato para a síntese do colágeno nos tecidos conjuntivos e nas cartilagens 11 , exatamente em virtude de sua composição aminoacídica atípica.…”

“…Oesser et al 11 demonstraram que peptídios de colágeno de até 15 -20 kDa puderam ser absorvidos a partir do hidrolisado. Foram usados peptídios marcados com carbono-14 ( 14 C) e hidrolisado não marcado, porém enriquecido com prolina ( 14 C), ao mesmo nível de radioatividade, tendo-se observado que a radioatividade da prolina (-14 C) livre e do hidrolisado (-14 C) distribuía-se igualmente no plasma e em vários outros tecidos.…”

“…Por outro lado, espera-se uma complementação das várias propriedades funcionais do WPI 5,7-9 com as do colágeno hidrolisado (HCB) [11][12][13] , na formulação de um complemento dietético para idosos.…”