RESUMO
: Seafood such as fish, shellfish, and squid are a unique source of nutrients. However, many marine processing byproducts, such as viscera, shells, heads, and bones, are discarded, even though they are rich sources of structurally diverse bioactive nitrogenous components. Based on emerging evidence of their potential health benefits, these components show significant promise as functional food ingredients. Fish waste components contain significant levels of high-quality protein, which represents a source for biofunctional peptide mining. The chitin contained in shrimp shells, crab shells, and squid pens may also be of value. The components produced by bioconversion are reported to have antioxidative, antimicrobial, anticancer, antihypertensive, antidiabetic, and anticoagulant activities. This review provides an overview of the extraordinary potential of processing fish and chitin-containing seafood byproducts via chemical procedures, enzymatic and fermentation technologies, and chemical modifications, as well as their applications.
Assuntos
Pesqueiros , Resíduos , Fenômenos Químicos , Manipulação de Alimentos , Alimentos Marinhos , Resíduos/análiseRESUMO
Protein kinase C (PKC) play critical roles in many cellular functions including differentiation, proliferation, growth, and survival. However, the molecular bases governing PKC's substrate recognitions remain poorly understood. Here we determined the structure of PKCι in complex with a peptide from Par-3 at 2.4 Å. PKCι in the complex adopts catalytically competent, closed conformation without phosphorylation of Thr402 in the activation loop. The Par-3 peptide binds to an elongated groove formed by the N- and C-lobes of the kinase domain. The PKCι/Par-3 complex structure, together with extensive biochemical studies, reveals a set of substrate recognition sites common to all PKC isozymes as well as a hydrophobic pocket unique to aPKC. A consensus aPKC's substrate recognition sequence pattern can be readily identified based on the complex structure. Finally, we demonstrate that the pseudosubstrate sequence of PKCι resembles its substrate sequence, directly binds to and inhibits the activity of the kinase.
Assuntos
Moléculas de Adesão Celular/química , Peptídeos/química , Proteína Quinase C/química , Proteínas Adaptadoras de Transdução de Sinal , Sequência de Aminoácidos , Animais , Sítios de Ligação , Moléculas de Adesão Celular/metabolismo , Proteínas de Ciclo Celular , Células HEK293 , Humanos , Interações Hidrofóbicas e Hidrofílicas , Isoenzimas/química , Isoenzimas/metabolismo , Camundongos , Modelos Moleculares , Dados de Sequência Molecular , Peptídeos/metabolismo , Fosforilação , Proteína Quinase C/metabolismo , Estrutura Terciária de Proteína , Especificidade por Substrato , TransfecçãoRESUMO
Skeletal muscle satellite cell-derived myoblasts are mainly responsible for postnatal muscle growth and injury-induced regeneration. However, the cellular signaling pathways that control proliferation and differentiation of myoblasts remain poorly defined. Recently, we found that JAK1/STAT1/STAT3 not only participate in myoblast proliferation but also actively prevent them from premature differentiation. Unexpectedly, we found that a related pathway consisting of JAK2, STAT2, and STAT3 is required for early myogenic differentiation. Interference of this pathway by either a small molecule inhibitor or small interfering RNA inhibits myogenic differentiation. Consistently, all three molecules are activated upon differentiation. The pro-differentiation effect of JAK2/STAT2/STAT3 is partially mediated by MyoD and MEF2. Interestingly, the expression of the IGF2 gene and the HGF gene is also regulated by JAK2/STAT2/STAT3, suggesting that this pathway could also promote differentiation by regulating signaling molecules known to be involved in myogenic differentiation. In summary, our current study reveals a novel role for the JAK2/STAT2/STAT3 pathway in myogenic differentiation.
