Rice starch is one of the major cereal starches with novel functional properties. Significant progress has been made in recent years on the characterization of rice starches separated from different rice cultivars. Studies have revealed that the molecular structure and functional properties are affected by rice germplasm, isolation procedure, climate, agronomic conditions, and grain development. Morphological studies (microscopy and particle size analysis) have reflected significant differences among rice starch granule shapes (polyhedral, irregular) and in granule size (2 to 7 μm). Nonwaxy and long-grain rice starches show greater variation in granular size than the waxy starches. Rice starch granules are smaller than other cereal starches with amylose contents varying from virtually amylose-free in waxy to about 35% in nonwaxy and long-grain rice starches. Amylose content appears to be the major factor controlling almost all physicochemical properties of rice starch due to its influence on pasting, gelatinization, retrogradation, syneresis, and other functional properties. Waxy rice starches have high swelling and solubility parameters, and larger relative crystallinity values than nonwaxy and long-grain starches. However, nonwaxy rice starches have a higher gelatinization temperature than the waxy and long-grain starches. The bland taste, nonallergenicity, and smooth, creamy, and spreadable characteristics of rice starch make it unique and valuable in food and pharmaceutical applications. This review provides recent information on the variation in the molecular structure and functional properties of different rice starches.

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Heparanase, the sole heparan sulfate degrading endoglycosidase, regulates multiple biological activities that enhance tumor growth, angiogenesis and metastasis. Heparanase expression is enhanced in almost all cancers examined including various carcinomas, sarcomas and hematological malignancies. Numerous clinical association studies have consistently demonstrated that upregulation of heparanase expression correlates with increased tumor size, tumor angiogenesis, enhanced metastasis and poor prognosis. In contrast, knockdown of heparanase or treatments of tumor-bearing mice with heparanase-inhibiting compounds, markedly attenuate tumor progression further underscoring the potential of anti-heparanase therapy for multiple types of cancer. Heparanase neutralizing monoclonal antibodies block myeloma and lymphoma tumor growth and dissemination; this is attributable to a combined effect on the tumor cells and/or cells of the tumor microenvironment. In fact, much of the impact of heparanase on tumor progression is related to its function in mediating tumor-host crosstalk, priming the tumor microenvironment to better support tumor growth, metastasis and chemoresistance. The repertoire of the physiopathological activities of heparanase is expanding. Specifically, heparanase regulates gene expression, activates cells of the innate immune system, promotes the formation of exosomes and autophagosomes, and stimulates signal transduction pathways via enzymatic and non-enzymatic activities. These effects dynamically impact multiple regulatory pathways that together drive inflammatory responses, tumor survival, growth, dissemination and drug resistance; but in the same time, may fulfill some normal functions associated, for example, with vesicular traffic, lysosomal-based secretion, stress response, and heparan sulfate turnover. Heparanase is upregulated in response to chemotherapy in cancer patients and the surviving cells acquire chemoresistance, attributed, at least in part, to autophagy. Consequently, heparanase inhibitors used in tandem with chemotherapeutic drugs overcome initial chemoresistance, providing a strong rationale for applying anti-heparanase therapy in combination with conventional anti-cancer drugs. Heparin-like compounds that inhibit heparanase activity are being evaluated in clinical trials for various types of cancer. Heparanase neutralizing monoclonal antibodies are being evaluated in pre-clinical studies, and heparanase-inhibiting small molecules are being developed based on the recently resolved crystal structure of the heparanase protein. Collectively, the emerging premise is that heparanase expressed by tumor cells, innate immune cells, activated endothelial cells as well as other cells of the tumor microenvironment is a master regulator of the aggressive phenotype of cancer, an important contributor to the poor outcome of cancer patients and a prime target for therapy.

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